Running Head: XLGs in heterotrimeric G protein signaling ... · 6 and siliques (Lease et al., 2001), as well as in pathogen responses (Llorente et al., 2005; Trusov et al., 2006;

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Running Head: XLGs in heterotrimeric G protein signaling

Corresponding author: Sarah M. Assmann

Biology Department

208 Mueller Laboratory

Pennsylvania State University

University Park, PA 16802, USA

Phone: 814-863-9579

Email: [email protected]

Plant Physiology Preview. Published on July 8, 2015, as DOI:10.1104/pp.15.00251

Copyright 2015 by the American Society of Plant Biologists

www.plantphysiol.orgon June 13, 2018 - Published by Downloaded from Copyright © 2015 American Society of Plant Biologists. All rights reserved.

http://www.plantphysiol.org

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Title: Extra-Large G proteins (XLGs) expand the repertoire of subunits in Arabidopsis heterotrimeric

G protein signaling

Authors: David Chakravorty2, Timothy E. Gookin2, Matthew J. Milner3, Yunqing Yu and Sarah M.

Assmann

Address:

Biology Department, 208 Mueller Laboratory, Pennsylvania State University, University Park,

PA 16802, USA

Summary The three extra-large GTP-binding proteins (XLG1, XLG2 and XLG3) function within the

Arabidopsis heterotrimeric G protein complex, increasing the diversity of possible heterotrimer

combinations.



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Footnotes 1 This research was supported by NSF grant MCB-1121612 to S.M.A., with additional support

from USDA/AFRI postdoctoral grant 2011-67012-30722 to M.J.M. 2 These authors contributed equally to the article. 3Current address of M.J.M: John Bingham Laboratory, National Institute for Agricultural Botany

(NIAB), Cambridge, CB3 0LE, United Kingdom.



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Abstract Heterotrimeric G proteins, consisting of Gα, Gβ and Gγ subunits, are a conserved signal

transduction mechanism in eukaryotes. However, G protein subunit numbers in diploid plant

genomes are greatly reduced as compared to animals, and do not correlate with the diversity of

functions and phenotypes in which heterotrimeric G proteins have been implicated. In addition to

GPA1, the sole canonical Arabidopsis thaliana Gα subunit, Arabidopsis has three related

proteins: the extra-large GTP-binding proteins XLG1, XLG2 and XLG3. We demonstrate that

the XLGs can bind Gβγ dimers (AGB1 plus a Gγ subunit: AGG1, AGG2, or AGG3) with

differing specificity, in yeast 3-hybrid assays. Our in silico structural analysis shows that XLG3

aligns closely to the crystal structure of GPA1, and XLG3 also competes with GPA1 for Gβγ

binding in yeast. We observed interaction of the XLGs with all three Gβγ dimers at the plasma

membrane in planta by BiFC. Bioinformatic and localization studies identified and confirmed

nuclear localization signals in XLG2 and XLG3, and a nuclear export signal in XLG3, which

may facilitate intracellular shuttling. We found that tunicamycin, salt, and glucose

hypersensitivity, and increased stomatal density are agb1 specific phenotypes that are not

observed in gpa1 mutants but are recapitulated in xlg mutants. Thus, XLG-Gβγ heterotrimers

provide additional signaling modalities for tuning plant G protein responses, and increase the

repertoire of G protein heterotrimer combinations from three to twelve. The potential for signal

partitioning and competition between the XLGs and GPA1 is a new paradigm for plant-specific

cell signaling.



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Introduction The classical heterotrimeric G protein consists of a GDP/GTP-binding Gα subunit with GTPase

activity, bound to an obligate dimer formed by Gβ and Gγ subunits. In the signaling paradigm

largely elucidated from mammalian systems, the plasma membrane-associated heterotrimer

contains Gα in its GDP bound form. Upon receiving a molecular signal, typically transduced by

a transmembrane protein (e.g. a G protein coupled receptor), Gα exchanges GDP for GTP and

dissociates from the Gβγ dimer. Both Gα and Gβγ interact with intracellular effectors to initiate

downstream signaling cascades. The intrinsic GTPase activity of Gα restores Gα to the GDP

bound form, which binds Gβγ, thereby reconstituting the heterotrimer (McCudden et al., 2005;

Oldham and Hamm, 2008).

Signal transduction through a heterotrimeric G protein complex is an evolutionarily conserved

eukaryotic mechanism common to metazoa and plants, although there are distinct differences in

the functional intricacies between the evolutionary branches (Jones et al., 2011a; Jones et al.,

2011b; Bradford et al., 2013). The numbers of each subunit encoded within genomes, and

therefore the potential for combinatorial complexity within the heterotrimer, is one of the most

striking differences between plants and animals. For example, the human genome encodes 23 Gα

(encoded by 16 genes), five Gβ and 12 Gγ subunits (Hurowitz et al., 2000; McCudden et al.,

2005; Birnbaumer, 2007). The Arabidopsis thaliana genome, however, only encodes one

canonical Gα (GPA1) (Ma et al., 1990), one Gβ (AGB1) (Weiss et al., 1994), and three Gγ

(AGG1, AGG2 and AGG3) subunits (Mason and Botella, 2000, 2001; Chakravorty et al., 2011),

while the rice genome encodes one Gα (Ishikawa et al., 1995), one Gβ (Ishikawa et al., 1996),

and either four or five Gγ subunits (Kato et al., 2004; Chakravorty et al., 2011; Botella, 2012).

As expected, genomes of polyploid plants have more copies due to genome duplication, with the

soybean genome encoding four Gα, four Gβ (Bisht et al., 2011) and 10 Gγ subunits (Choudhury

et al., 2011). However, Arabidopsis heterotrimeric G proteins have been implicated in a

surprisingly large number of phenotypes, which is seemingly contradictory given the relative

scarcity of subunits. Arabidopsis G proteins have been implicated in cell division (Ullah et al.,

2001; Chen et al., 2006) and morphological development in various tissues including hypocotyls

(Ullah et al., 2001; Ullah et al., 2003), roots (Ullah et al., 2003; Chen et al., 2006; Li et al.,

2012), leaves (Lease et al., 2001; Ullah et al., 2001), inflorescences (Ullah et al., 2003), flowers



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and siliques (Lease et al., 2001), as well as in pathogen responses (Llorente et al., 2005; Trusov

et al., 2006; Cheng et al., 2015), regulation of stomatal movement (Wang et al., 2001; Coursol et

al., 2003; Fan et al., 2008) and development (Zhang et al., 2008; Nilson and Assmann, 2010),

cell wall composition (Delgado-Cerezo et al., 2012), responses to various light stimuli (Warpeha

et al., 2007; Botto et al., 2009), responses to multiple abiotic stimuli (Huang et al., 2006; Pandey

et al., 2006; Trusov et al., 2007; Zhang et al., 2008; Colaneri et al., 2014), responses to various

hormones during germination (Ullah et al., 2002), and post-germination development (Ullah et

al., 2002; Pandey et al., 2006; Trusov et al., 2007). Since the Gγ subunit appeared to be the only

subunit that provides diversity in heterotrimer composition in Arabidopsis, it was proposed that

all functional specificity in heterotrimeric G protein signaling was provided by the Gγ subunit

(Trusov et al., 2007; Chakravorty et al., 2011; Thung et al., 2012; Thung et al., 2013). This

allowed for only three heterotrimer combinations to account for the wide range of G protein-

associated phenotypes.

In addition to the above typical G protein subunits, the plant kingdom contains a conserved

protein family of extra-large GTP-binding proteins (XLGs). XLGs differ from typical Gα

subunits in that they possess a long N-terminal extension of unknown function, but they are

similar in that they all have a typical C-terminal Gα-like region, with five semi-conserved G-box

(G1 to G5) motifs. The XLGs also possess the two sequence features that differentiate

heterotrimeric G protein Gα subunits from monomeric G proteins: a helical region between the

G1 and G2 motifs and an aspartate/glutamate-rich loop between the G3 and G4 motifs, (Lee and

Assmann, 1999; Ding et al., 2008; Heo et al., 2012). The Arabidopsis XLG family comprises

XLG1, XLG2, and XLG3, and all three have demonstrated GTP-binding and GTPase activity,

although they differ from GPA1 in exhibiting a much slower rate of GTP hydrolysis, with a Ca2+

cofactor requirement, instead of a Mg2+ requirement as for canonical Gα proteins (Heo et al.,

2012). All three Arabidopsis XLGs were observed to be nuclear localized (Ding et al., 2008).

Though much less is known about XLGs than canonical Gα subunits, XLG2 positively regulates

resistance to the bacterial pathogen Pseudomonas syringae, and was immunoprecipitated with

AGB1 from tissue infected with P. syringae (Zhu et al., 2009). xlg3 mutants, like agb1 mutants,

are impaired in root waving and root skewing responses (Pandey et al., 2008). During

preparation of this report, Maruta et al. (2015) further investigated XLG2, particularly focusing



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on the link between XLG2 and Gβγ in pathogen responses. Based on symptom progression in xlg

mutants, they found that XLG2 is a positive regulator of resistance to both bacterial and fungal

pathogens, with a minor contribution from XLG3 in resistance to Fusarium oxysporum. XLG2

and XLG3 are also positive regulators of ROS production in response to pathogen-associated

molecular pattern (PAMP) elicitors. The resistance and PAMP-induced ROS phenotypes of the

agg1 agg2 and xlg2 xlg3 double mutants were not additive in an agg1 agg2 xlg2 xlg3 quadruple

mutant, indicating that these two XLGs and the two Gγ subunits function in the same, rather than

parallel, pathways. Unfortunately, the close proximity of XLG2 and AGB1 on chromosome 4

precluded generation of an agb1 xlg2 double mutant therefore, direct genetic evidence of XLG2

and AGB1 interaction is still lacking, but physical interactions between XLG2 and the Gβγ

dimers were shown by yeast 3-hybrid and BiFC assays (Maruta et al., 2015). Localization of all

three XLGs was also re-examined, indicating that XLGs are capable of localizing to the plasma

membrane, in addition to the nucleus (Maruta et al., 2015).

Interestingly, several other plant G protein-related phenotypes, in addition to pathogen

resistance, have been observed only in Gβ and Gγ mutants, with opposite phenotypes observed in

Gα (gpa1) mutants. Traditionally, observation of opposite phenotypes in Gα vs. Gβγ mutants in

plants and other organisms has mechanistically been attributed to signaling mediated by free

Gβγ, which increases in abundance in the absence of Gα. However, an intriguing alternative is

that XLG proteins fulfill a Gα-like role in forming heterotrimeric complexes with Gβγ, and

function in non-GPA1-based G protein signaling processes. If XLGs function like Gα subunits,

the corresponding increase in subunit diversity could potentially account for the diversity of G

protein phenotypes. In light of this possibility, we assessed the heterotrimerization potential of

all possible XLG and Gβγ dimer combinations, XLG localization and its regulation by Gβγ, and

the effect of xlg mutation on selected known phenotypes associated with heterotrimeric G

proteins. Our results provide compelling evidence for the formation of XLG-Gβγ heterotrimers,

and reveal that plant G protein signaling is substantially more complex than previously thought.

Results

XLG-Gβγ interaction in vivo



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Maruta et al. (2015) previously reported that XLG2 interacts with AGB1/AGG1, AGB1/AGG2

and AGB1/AGG3 in yeast 3-hybrid assays, but they did not test the ability of XLG1 or XLG3 to

interact with any of the Gβγ dimers. We tested all three XLGs against all three Gβγ dimers.

Evidence for a transmembrane domain in AGG3, which would place the C-terminus of AGG3

outside of the cell (Wolfenstetter et al., 2015), was taken into consideration by including an

additional AGB1/AGG3 construct (designated Gβγ(γ)), in which only the Gγ-like domain

(residues 1-112) of AGG3 was fused to the GAL4 binding domain. We also investigated

interaction strength within the complexes, wherein growth on higher concentrations of 3-amino-

1,2,4-triazole (3-AT) is an accepted indicator of a stronger or more stable interaction (Durfee et

al., 1993; Ursic et al., 2004).

The interaction between GPA1 and Gβγ dimers containing AGG1 or AGG2 was quite weak,

with yeast growth observed only in the absence of 3-AT. The only dimer with which GPA1

showed a strong interaction was AGB1/AGG3(γ) (Fig. 1A). XLG1 and XLG2 interaction with

Gβγ dimers containing AGG1 or AGG2 (Fig. 1, B and C) was stronger than that of GPA1.

XLG1 and XLG2 did not interact in yeast with Gβγ dimers containing AGG3 (Fig. 1, B and C);

however, XLG3 interacted strongly with all Gβγ dimers, including those containing AGG3 (Fig.

1D). Therefore, we found strong evidence from this approach for interaction of eight of the 12

heterotrimeric complexes tested.

In the above assays, the XLGs or GPA1 were fused to the GAL4 activation domain, the Gγ

subunits (AGG1, AGG2 or AGG3) were fused to the GAL4 binding domain (MCS1 of the yeast

3-hybrid vector pBridge), and AGB1 was used as the bridge protein, expressed from MCS2 of

pBridge. Therefore, it was possible that the yeast reporter genes were activated by direct

interaction between each XLG and each Gγ subunit. To assess whether the yeast 3-hybrid

interactions do in fact involve a heterotrimeric interaction, i.e. with a requirement for AGB1, the

AGB1 bridge protein was not included, and the assay was repeated. As shown in Figure 2, co-

expression of the Gβ subunit, AGB1, was required for interaction. These results raised the

hypothesis that GPA1 and the XLGs may compete with each other for Gβγ-binding. Since XLG1

and XLG2 did not bind the same Gβγ dimers as GPA1 in yeast (Fig. 1), XLG3 and

AGB1/AGG3(γ) were selected to test this hypothesis. Either GPA1 or XLG3 was expressed



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under the control of the strong GPD promoter (Bitter and Egan, 1984; Partow et al., 2010), in

competition with the GAL4:XLG3 or GAL4:GPA1 activation domain fusions, respectively.

XLG3 was able to inhibit GPA1-AGB1/AGG3 interaction, and GPA1 was able to inhibit XLG3-

AGB1/AGG3 interaction (Fig. 3).

XLG three-dimensional (3-D) structure analysis in silico The ability of all three XLGs to interact with Gβγ dimers, and of XLG3 to compete with GPA1

in yeast, suggests that all four G proteins are structurally similar. As seen in the alignment of

Ding et al. (2008), primary sequence conservation between GPA1 and the XLG proteins is

moderate, with percent identities of GPA1 and the XLG Gα-domains of 26.1%, 23.2%, and

28.5% for XLG1446-888, XLG2435-861, and XLG3396-848, respectively. Therefore, we performed an

in silico analysis of each XLG using Phyre2 (Kelley and Sternberg, 2009), which generates a

protein fold profile for subsequent analysis by the secondary structure predictor Psi-Pred (Jones,

1999b). Phyre2 then identifies similar tertiary structures in a fold library via profile-profile

alignments (Kelley and Sternberg, 2009). The top 20 in silico structural matches for all three

XLGs corresponded to heterotrimeric G protein Gα subunits, including GPA1 (Supplemental

Table S1), with 99.9% to 100% confidence, and the conserved secondary structure patterning of

the XLGs and GPA1 is evident when the Phyre2 data are superimposed over an alignment of

their Gα regions (Supplemental Fig. S1). As an independent secondary confirmation, the

genTHREADER software was used to conduct additional fold recognition analyses (Jones,

1999a). genTHREADER returned 13 hits for each of the three XLGs that were classed as either

‘certain’ (p-value <0.0001) or ‘high’ (p-value = 0.0001-0.001), all of which corresponded to the

same 13 heterotrimeric G protein Gα structures, including that of GPA1 (Supplemental Table

S2). In contrast to the high confidence matching of the C-terminal domains of the XLGs with

canonical Gα subunit structures, there were no high ranking hits that matched the N-terminal

domains of the XLGs.

We next examined the Gα region of XLG3 in greater detail by utilizing the I-TASSER server for

protein structure modeling, assigning the empirically resolved crystal structure of GPA1

(PDB:2XTZ:A) (Jones et al., 2011a) as a template. For reference, the XLG3 Gα region

encompasses residues 429-849, with residue 429 aligning to GPA1 residue 37 (Supplemental



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Fig. S1). To allow direct correlation, the exogenous MSGI tetrapeptide found at the N-terminus

of the GPA1 2XTZ crystal structure (Jones, 1999a) was computationally affixed to the XLG3 Gα

domain; therefore, the first XLG3 native residue corresponds to residue number 5 in the

XLG3alpha.pdb structure (Supplemental File 1). The predicted XLG3 structure aligned closely

to the crystal structure of GPA1 (Fig. 4 and Supplemental Fig. S2). The theoretical model of the

XLG3 Gα domain was validated as a reasonable approximation of the as yet undescribed XLG3

crystal structure, with a passing self-compatibility score (82.55% of residue 3D-1D score ≥ 0.2)

from Verify-3D (Eisenberg et al., 1997), a ProSA Z-score of -7.2, (Supplemental Fig. S3)

(Wiederstein and Sippl, 2007), and a plausible overall quality score of 83.894 (Supplemental Fig.

S4) from ERRAT (Colovos and Yeates, 1993), which is designed to verify protein structures

empirically determined from crystallography data. Together, the Phyre2 and genTHREADER

identification of structural homology to metazoan and plant Gα subunits, and the close alignment

of the XLG3 and GPA1 Gα regions by I-TASSER, support XLG function as a component of the

plant heterotrimeric G protein.

XLG-Gβγ interaction in planta To further test the hypothesis that XLGs function as Gα subunits, we utilized our recently

developed multi-cassette pDOE vector BiFC system (Gookin and Assmann, 2014) with reduced

non-specific signal from self-assembly (Ohashi et al., 2012; Gookin and Assmann, 2014), to

evaluate the XLG-Gβγ interactions in planta and assess sub-cellular localization. GPA1 interacts

with AGB1-AGG dimers (Gookin and Assmann, 2014) when tagged internally, in a

configuration consistent with a mammalian heterotrimer crystal structure (McCudden et al.,

2005). Given the results of our yeast 3-hybrid competition assay, we hypothesized that the XLGs

and GPA1 would interact similarly with AGB1-AGG dimers. Accordingly, we inserted the

NmVenus210 fragment into the middle of each XLG protein at a position analogous to the αB-

αC loop of GPA1 (Fig. 4) to generate XLG1L, XLG2L, and XLG3L “parent vectors”, to which

AGB1 was added to create three XLGL—CVen210:AGB1 test vectors. Negative control assays

with the XLGL parent vectors (with an unfused CVen210 fragment in the second cassette) did

not show any non-specific BiFC signal (Fig. 5, A, F and K). The XLGL—CVen210:AGB1 test

constructs also showed zero to near zero signal (Fig. 5, B, G and L). In all cases, positive

transformation was confirmed by a vector-integrated XT-Golgi-mTq2 marker. Positive



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interaction between each XLGL fusion and AGB1 was only obtained when exogenous untagged

AGG1 (Fig. 5, C, H and M), AGG2 (Fig. 5, D, I and N), or AGG3 (Fig. 5, E, J and O) subunits

were provided via co-transformation with a second vector. Population level images show the

reproducibility of these assays (Supplemental Fig. S5).

To identify the subcellular localization of the XLG-AGB1-AGG heterotrimers, we performed

high magnification (63x and 95x) co-localization experiments with the plasma membrane

staining dye, FM4-64 (Bolte et al., 2004), and found that the interaction occurs specifically at the

plasma membrane (Fig. 6). Furthermore, the XLG-Gβγ heterotrimers do not co-localize with

internalizing FM4-64 labeled vesicles (Fig. 6, J, K and L). These results complement our yeast

data, and show a dependency on all three subunits for a positive XLG-AGB1 interaction at the

plasma membrane in planta.

XLG subcellular localization All three Arabidopsis XLG proteins were originally described as nuclear resident proteins (Ding

et al., 2008), but Murata et al. (2015) showed XLG1 localization at the plasma membrane and

XLG2 and XLG3 localization at both the plasma membrane and nucleus.

To re-assess XLG subcellular localization patterns, we created Ubiquitin10 promoter-driven

XLG:mVenus fusions. We reasoned that the use of the optimized and bright monomeric mVenus

fluoroprotein, in combination with the slower kinetics of the Ubiquitin10 promoter-driven

expression, would allow for enhanced temporal resolution (Gookin and Assmann, 2014).

Analysis of XLG:mVenus fusions transiently expressed in Nicotiana benthamiana leaves

showed that XLG1 is primarily extra-nuclear, with nuclear signal ranging from not detectable to

weak (Fig. 7, A and B). XLG2:mVenus localization varied from predominately nuclear (Fig.

7C), to an even distribution between nucleus and the cytoplasm (Fig. 7D). XLG3:mVenus

consistently localized to both the nucleus and cytoplasm (Fig. 7, E and F), in every

agroinfiltration experiment. The nuclear accumulation patterns of the three XLGs were

confirmed in high-magnification (63x) co-localization experiments, with mTq2 tagged nuclear

specific Histone 2B (Heidstra et al., 2004) co-localizing with the XLGs in the nucleus

(Supplemental Fig. S6). In comparison, our BiFC results show that all three XLGs interact with



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all three Gβγ dimers at the cell periphery (Fig. 5 and Supplemental Fig. S5), suggesting that co-

expression of partner subunits is a key determinant of XLG intracellular location.

Sequence analysis of the three XLGs using the PredictProtein software suite (Yachdav et al.,

2014) only identified the classic monopartite NLS present in XLG3 (RRKKKKK), previously

identified by Ding et al. (2008). We next used computational regular expressions to search the

set of NLS identified and functionally characterized in BY-2 tobacco cells by Kosugi et al.

(2009). Our search identified a potential non-canonical NLS in XLG2 (KKRAKiaCAVF),

through a partial match with CAVF (Fig. 8A). This potential XLG2 NLS resides within a small

stretch of sequence that is semi-conserved among the XLGs (Fig. 8B). Accordingly, we assessed

the NLS functionality of this region. We used residue substitution to modify the XLG1 sequence

to mirror XLG2 in this stretch (arrows in Fig. 8B), and expressed the resultant XLG1m1:mVenus

fusion in N. benthamiana leaves. In contrast to XLG1 (Fig. 7, A and B, and Supplemental Fig.

S6A), XLG1m1 produced strong nuclear signal (Fig. 8C), specifically co-localizing with the

nuclear specific signal of mTq2:Histone 2B (Fig. 8, D and F), and providing evidence that the

atypical NLS of XLG2 is functional.

Since XLG2 and XLG3 also show both nuclear and extra-nuclear localization, we analyzed these

sequences in search of a nuclear export signal (NES). We did not find a direct match to the

classic consensus pattern for a leucine-rich NES (Xu et al., 2012), therefore we used

computational regular expressions to search the set of validated NES identified by Kosugi et al.

(2008). Our analyses based on hydrophobic residue spacing identified a potential unconventional

class 2 NES in XLG3 (LELRILKL) (Fig. 9A). Two of these residues (I and the final L) were also

weakly identified by NetNES (la Cour et al., 2004), suggesting the presence of a NES. We

created two residue substitution mutants to map the domain, in which conserved hydrophobic

residues that are functionally important to the motif were substituted with glycine (lower case g):

XLG3m1:mVenus (gEgRILKL) and XLG3m2:mVenus (LELRggKg) (Fig. 9A). Both XLG3m1

and XLG3m2 produced strong nuclear signal (Fig. 9, B, C and-D), demonstrating that the

identified NES regulates XLG3 subcellular localization.



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We next investigated XLG3:mVenus localization upon co-expression of 35S-driven untagged

AGB1-AGG1 and AGB1-AGG2 dimers. In both assays, XLG3 was sequestered at the plasma

membrane, and in many cases the nucleus was devoid of fluorescent signal (Fig. 10). These

results provide evidence that XLG3 localization is dynamic and, in conjunction with our BiFC

results, demonstrate that the plasma membrane is the site of XLG-Gβγ interaction.

xlg mutants recapitulate agb1/agg1 and agb1/agg2 phenotypes The majority of G protein related phenotypes have been characterized for gpa1 and agb1

mutants; however, for a growing but not yet comprehensive number of phenotypes, details have

been described for Gγ subunit mutants as well. Comparison of published phenotypes suggests

that while AGB1 (the only Gβ subunit) participates in all G protein-mediated processes, the

majority of gpa1 phenotypes are restricted to recapitulation in agg3 mutants. For example,

hypersensitivity to ABA during germination (Ullah et al., 2002; Chakravorty et al., 2011),

decreased etiolated hypocotyl elongation (Ullah et al., 2001; Chakravorty et al., 2011), round leaf

morphology (Ullah et al., 2001; Chakravorty et al., 2011), hyposensitivity to ABA inhibition of

stomatal opening (Wang et al., 2001; Chakravorty et al., 2011), shortened silique morphology

(Trusov et al., 2008; Chakravorty et al., 2011) and round seed (Chakravorty et al., 2011)

phenotypes are all similar in gpa1 and agg3 mutants. The recapitulation of gpa1 phenotypes in

agg3 mutants correlates well with the GPA1-AGB1/AGG3 binding specificity demonstrated in

Figure 1. Conversely, a number of agg1 and agg2 phenotypes are recapitulated in agb1, but

opposite or wild-type phenotypes are observed in gpa1 mutants (Table 1). Our yeast 3-hybrid

results, showing that AGB1/AGG1 and AGB1/AGG2 interact preferentially with XLGs over

GPA1, raise the intriguing possibility that XLGs form signaling complexes with Gβγ, and may

especially be involved in agb1/agg1 and agb1/agg2 phenotypes. We selected several phenotypes

present in agb1 mutants, but absent from (or not yet assessed in) gpa1 mutants, for examination

in xlg mutants. The four phenotypes we selected were NaCl, tunicamycin and glucose

hypersensitivity, and increased stomatal density.

Colaneri et al. (2014) showed that Arabidopsis agb1 mutants are hypersensitive to NaCl, while

gpa1 is hyposensitive to NaCl. Urano et al. (2014) examined Gα mutants available in rice and

maize, and found that the Gα mutants were, much like gpa1 mutants in Arabidopsis,



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hyposensitive to salt treatment. The hypersensitivity of Gβ mutants to NaCl, and the

hyposensitivity of Gα mutants, suggested that NaCl sensitivity is a candidate for a potential xlg

phenotype. Colaneri et al. (2014) found that agg1 and agg2 single mutants were not

hypersensitive to NaCl; however, the agg1-1c agg2-1 agg3-1 triple mutant appeared

hypersensitive to NaCl.

As we hypothesize that agg1- and/or agg2-mediated phenotypes are a potential indicator of XLG

involvement, we first clarified Gγ subunit involvement in NaCl sensitivity by testing all single,

double, and triple mutant combinations of Gγ mutants, and deduced that AGG1 and AGG2 play

redundant roles in NaCl sensitivity: agg1-1c agg2-1 double mutants displayed a similar NaCl

hypersensitivity as the agb1-2 mutant, or the agg triple mutant (Fig. 11A). AGG3 is not involved

in salt sensitivity, as all agg3 containing genotypes, aside from the agg triple mutant, displayed

wild-type sensitivity (Fig. 11A). We next investigated the salinity phenotype of the xlg single

and triple mutants. An increased number of xlg single mutant seedlings, as compared to wild-

type seedlings, displayed slight chlorosis, indicated by arrows in Figure 11B, on 150 mM NaCl

plates. The chlorosis was generally limited to one or two leaves in the single xlg mutants, and

was much more pronounced in both the agb1-2 mutant and the xlg triple mutant (Fig. 11B).

Similarly, when compared to wild-type, the agb1-2 and xlg triple mutants each displayed a clear

decrease in seedling survival (Fig. 11C). Therefore, the agb1-2, agg1-1c agg2-1 double, and xlg

triple mutants displayed similar NaCl hypersensitivity phenotypes, suggesting the possibility that

up to six heterotrimer combinations, XLG1/AGB1/AGG1, XLG1/AGB1/AGG2,

XLG2/AGB1/AGG1, XLG2/AGB1/AGG2, XLG3/AGB1/AGG1 and XLG3/AGB1/AGG2,

function in salt sensitivity.

Another potential xlg phenotype is hypersensitivity to tunicamycin, a mixture of homologous

compounds that block N-linked glycosylation, thereby inducing the unfolded protein response

(UPR) (Schroder and Kaufman, 2005), a stress response initiated in the ER when the cellular

protein production and folding machinery is overcome, for example by inhibited post-

translational modification (Koizumi et al., 2001; Schroder and Kaufman, 2005). Wang et al.

(2007) initially reported that the agb1-2 mutant was hyposensitive to tunicamycin, while gpa1-4

displayed wild-type sensitivity. Contrary to the initial report, Chen and Brandizzi (2012) reported



15

that multiple agb1 mutants, including agb1-2, were hypersensitive to tunicamycin in a plate-

based seedling assay assessing recovery from tunicamycin. Similar to the report from Chen and

Brandizzi (2012), in our hands, agb1-2 was more sensitive than wild-type to tunicamycin, with

0.15 µM tunicamycin the optimal concentration for differentiating agb1-2 from wild-type.

We then investigated the Gγ subunit mutants in the tunicamycin recovery assay. The agg1-1c

agg2-1 double mutant and agg triple mutant, like agb1-2, were particularly hypersensitive to

tunicamycin. As with the salt assay, the gpa1 and single Gγ mutants were not hypersensitive to

tunicamycin (Fig. 12A), suggesting that AGG1 and AGG2 play redundant roles, and that

tunicamycin sensitivity is a candidate xlg phenotype. As seen in Figure 12B, the xlg single

mutants, particularly xlg2-1 and xlg3-1, were indeed hypersensitive to tunicamycin, showing a

clear increase in the number of stunted seedlings, as compared to wild-type (Fig. 12, B and C).

The xlg triple mutant fully recapitulated the agb1-2 hypersensitivity phenotype, with ~90% of

seedlings of both genotypes unable to recover from the treatment (Fig. 12B) and scored as dead

(Fig. 12C). The similarity of tunicamycin hypersensitivity phenotypes suggests that the XLGs

may function in a heterotrimer with AGB1/AGG1 and AGB1/AGG2.

A third potential xlg phenotype is the sensitivity of agb1 to glucose in post-germination

development. It has been demonstrated that agb1-2 is hypersensitive to D-glucose when grown

on plates (Wang et al., 2006). Additionally, the Arabidopsis Regulator of G protein Signaling

protein, AtRGS1, has been implicated in D-glucose signaling, as rgs1 seedlings are

hyposensitive to D-glucose (Chen and Jones, 2004), and AtRGS1 internalizes upon D-glucose

treatment in an AGB1- and AGG1-/AGG2-dependent manner (Urano et al., 2012b). We

germinated seeds of the G protein mutants on media supplemented with 1% or 6% glucose under

high light conditions to synchronize germination (Trusov et al., 2007), then allowed seedlings to

grow under low light conditions, to replicate the assay conducted by Wang et al. (2006).

However, in our hands, even 6% glucose was not sufficient to severely repress seedling

development of agb1-2 seedlings. Instead, the increased stress placed upon the agb1-2 seedlings

manifested in increased anthocyanin production at higher glucose concentrations; therefore, we

quantitatively assessed the glucose stress phenotype by measuring anthocyanin content

(Mancinelli et al., 1991).



16

Anthocyanin content of all genotypes was similarly negligible when grown on media

supplemented with 1% glucose (Fig. 13, A and B). However, anthocyanin content in 6% glucose

was elevated in agb1-2 and all agg1-1c containing genotypes (agg1-1c, agg1-1c agg2-1, agg1-1c

agg3-1 and the agg triple mutant), but not in gpa1-4 (Fig. 13A). Therefore, glucose sensitivity

fits the criteria of an agb1/agg1 or agb1/agg2 phenotype that lacks GPA1 involvement. When

we repeated the assay with xlg mutants, the xlg triple mutant reproduced the agb1-2 phenotype

(Fig. 13B). These results suggest that XLG/AGB1/AGG1 heterotrimers function in post-

germination glucose sensitivity.

Finally, we investigated the stomatal density phenotype of the G protein mutants. Zhang et al.

(2008) found that gpa1 and agb1 mutants displayed a lower and higher stomatal density than

wild-type, respectively, in cotyledons. Chakravorty et al. (2011) showed that the agg3 mutants

resembled wild-type in cotyledon stomatal density. These results suggested that stomatal density

is another candidate phenotype for XLG involvement.

The cotyledons of gpa1 and agb1 mutants displayed lower and higher stomatal density than wild

type (Fig. 14, A, C, D and E), respectively, in agreement with the results of Zhang et al. (2008).

As seen in Figure 14A, the agg1-1c mutant also displayed an increase in stomatal density, as did

the agg1-1c agg2-1 double mutant, and the agg triple mutant. Of the Gγ mutants, the agg1-1c

agg2-1 double mutant displayed the largest increase in stomatal density, higher even than agb1

or the agg triple mutant. All agg3-containing genotypes displayed a slight, but not statistically

significant, decrease in stomatal density as compared to wild-type. Like the agb1 mutant, the xlg

triple mutant displayed an increase in stomatal density (Fig. 14, B, C, E and F), indicating that

XLG/AGB1/AGG1,2 heterotrimers repress stomatal development. In fact the stomatal density of

the xlg triple mutant was greater than that of the agb1 mutant (P = 0.02, Student’s t-test). These

results may indicate a dual function for AGB1, with GPA1/AGB1/AGG3 heterotrimers

stimulating stomatal development, and XLG/AGB1/AGG1 and XLG/AGB1/AGG2

heterotrimers repressing stomatal development. This would explain the greater severity of the

agg1-1c agg2-1 (Fig. 14A) and xlg triple (Fig.14B) mutants when compared to agb1 and the agg

triple mutant.



17

Discussion

XLGs as non-canonical Gα proteins Here we make a case that the three XLGs are non-canonical Gα subunits that function within the

heterotrimeric G protein complex. The sole canonical Gα protein subunit in Arabidopsis is

GPA1, originally identified by Ma et al. (1990) in 1990. In 1999, we reported identification of

the first non-canonical Gα-like protein in plants, Arabidopsis XLG1, and we demonstrated that

the XLG1 protein binds GTP (Lee and Assmann, 1999). Analysis by Maruta et al. (2015)

suggests that XLGs evolved from canonical Gα subunits. Furthermore, our in silico structural

analysis shows that the XLG3 Gα domain and GPA1 are strikingly similar (Fig. 4 and

Supplemental Figures S1 and S2), suggesting that GPA1 and XLG3 may share a common

binding surface on Gβγ. The intermolecular arrangement of canonical Gα with Gβγ in the

heterotrimer is well established (Wall et al., 1998), and all three XLG family members show

strong structural conservation of their Gα region with the empirically derived GPA1 structure

(Supplemental Tables S1 and S2). In our yeast 3-hybrid assays, we observed that GPA1 and

XLG3 are capable of competing with each other for binding of the AGB1/AGG3 dimer (Fig. 3).

Competition between GPA1 and XLG3 for Gβγ-binding also suggests that GPA1 and XLG3

share a common binding surface on Gβγ, supporting the hypothesis that XLGs and GPA1 bind

Gβγ in a similar conformation. This idea is further supported by the efficient interaction between

XLGs and Gβγ dimers that is observed (Fig. 5) upon insertion of the NmVenus210 fragment into

a position analogous to the αB-αC loop insertion; a position that also enables observation of

GPA1 interaction with AGB1-AGG dimers in BiFC (Gookin and Assmann, 2014). Our protein-

protein interaction data and phenotypic analyses, in combination with the genetic evidence

provided by Maruta et al. (2015), suggest the recapitulation of agb1 phenotypes that we observe

in the xlg triple mutant is likely due to the XLGs, AGB1, and AGG1/AGG2 functioning in the

same pathways. In short, we provide evidence from several different approaches that all three

XLG proteins participate within a heterotrimeric G protein complex.

One impediment to denoting XLGs as true Gα subunits relates to the fact that bona fide Gα

subunits display a GTP/GDP switch during the activation/inactivation cycle, and that while

XLGs are GTP-/GDP-binding and GTPase capable proteins (Heo et al., 2012), this switch has



18

not been shown to control activation/inactivation. However, in truth the single canonical

Arabidopsis Gα subunit, GPA1, also falls short of fulfilling this stringent criterion. The

activation/inactivation dynamics of GPA1 are poorly understood, due to unusual GTP binding

and hydrolysis kinetics (Johnston et al., 2007; Johnston et al., 2008; Urano et al., 2012a),

regulation by the atypical 7-TM AtRGS1 (Chen et al., 2003; Jones et al., 2011b; Urano et al.,

2012b), and functional interactions between RLKs and G proteins (Bommert et al., 2013; Liu et

al., 2013; Ishida et al., 2014). Indeed, the in planta GTP-/GDP-binding kinetics of GPA1, as well

as those of the XLGs, are unknown. Because Gβγ availability may alter the ratio of GTP-bound

vs. GDP-bound Gα subunits, the addition of XLGs as potentially competing Gβγ interactors may

have implications for the in planta activity of the Gα pool, including GPA1.

It should be noted that we provide direct evidence for GPA1 and XLG3 competition for Gβγ-

binding only in yeast; it would be valuable to perform analogous experiments in planta as well.

Such experiments may be technically challenging, given previously noted difficulties in

expressing tagged XLG protein at adequate levels for such assessments (Ding et al., 2008).

While competition between GPA1 and XLGs for Gβγ could be a common theme, it is also

possible that XLG- and GPA1-based heterotrimers modulate shared molecular signaling

pathways. GPA1 interacts with: GCR1, the only putative Arabidopsis G protein coupled receptor

(GPCR) based on sequence and structural homology (Plakidou-Dymock et al., 1998; Pandey and

Assmann, 2004; Warpeha et al., 2007; Taddese et al., 2014), GTG1/GTG2, the two Arabidopsis

GPCR-type G proteins (Pandey et al., 2009), and RGS1, the sole demonstrated Gα GTPase

activating protein (GAP) in Arabidopsis (Chen et al., 2003). The potential interactions of the

XLGs with these signaling elements remain to be explored.

Interaction of XLG proteins with Gβγ dimers in vivo The interaction of one of the XLGs, XLG2, with Gβγ was shown by yeast 3-hybrid and

confirmed by BiFC by Maruta et al. (2015), but interaction strength was not investigated. We

now demonstrate that all three XLGs bind Gβγ dimers, with distinct specificity, and with

differences in binding strength in the yeast 3-hybrid system. The canonical Gα subunit, GPA1,

displayed a preference for AGB1/AGG3(γ) over AGB1/AGG1 or AGB1/AGG2 (Fig. 1A).

Similarly strong, or even stronger interactions than that of GPA1 with AGB1/AGG3(γ), were



19

observed for several of the XLG-Gβγ interactions (Fig. 1). The fact that XLG interactions with

Gβγ dimers are as strong as or stronger than the Gβγ interactions of the canonical GPA1 is

evidence that XLGs function in the heterotrimer.

There were some slight discrepancies between the yeast 3-hybrid results of Maruta et al. (2015),

and our yeast 3-hybrid data. For example, Maruta et al. (2015) obtained positive results using

XLG2, AGB1, and an untagged AGG3 subunit, whereas our results were negative using XLG2

and AGG3, with untagged AGB1 as the bridge protein (Fig. 1C). One explanation is that the

XLG2-AGB1/AGG3 interaction is extremely weak, and fell below the detectable threshold in

our conditions and assay configuration. It also should be noted that negative yeast 3-hybrid

results are not always definitive for lack of interaction. For example, we did not see strong

evidence for GPA1/AGB1/AGG1 or GPA1/AGB1/AGG2 heterotrimers in yeast, yet gpa1, agb1,

and agg1-1c agg2-1 mutants all display hypersensitivity to glucose repression of germination

(Ullah et al., 2002; Pandey et al., 2006; Trusov et al., 2007), functionally implicating complexes

of these subunits in planta. As GPA1/AGB1/AGG1 and GPA1/AGB1/AGG2 heterotrimers have

been observed in planta by BiFC (Gookin and Assmann, 2014), formation of these heterotrimers

likely requires plant-specific co-factors.

Maruta et al. (2015) previously showed that XLG2 interacted with all three Arabidopsis Gβγ

dimers by BiFC. However, the use of “sticky” N-173 based split eYFP fragments (Kodama and

Hu, 2012) coupled with strong expression driven by the double 35S promoter present in the

pSAT vectors, and a relatively long protoplast incubation time of 16-24 hours, could confound

results (Maruta et al., 2015). To assess XLG-Gβγ heterotrimer formation, we performed BiFC

for all three XLGs using the pDOE low background BiFC system (Gookin and Assmann, 2014).

Our results show that all three XLGs interact with AGB1/AGG1, AGB1/AGG2, and

AGB1/AGG3 at the plasma membrane (Figs. 5 and 6), with a signal localization pattern

reminiscent of the GPA1-Gβγ BiFC signal (Gookin and Assmann, 2014). Importantly, no BiFC

signal was observed in the absence of a co-expressed Gγ subunit, demonstrating, as in our yeast

3-hybrid results, that the XLG-Gβ interaction is not bipartite, and that true heterotrimer

formation occurs. This contrasts with data from Maruta et al. (2015), which showed BiFC signal

between XLG2 and the three Gγ subunits in agb1 protoplasts. One possible explanation is that



20

XLG2 and the Gγ subunits exist in a complex strong and stable enough (without AGB1) to allow

detectable BiFC. Alternatively, the BiFC signal observed by Maruta et al. (2015) could have

arisen from non-specific self-assembly of the BiFC fragments, as outlined above.

XLG localization The previously described subcellular localization of XLGs in the nucleus and Gβγ dimers at the

plasma membrane could provide an impediment to the hypothesis that XLGs function as

heterotrimeric G protein subunits, although AGB1 localization to the nucleus has also been

reported, albeit without an equivalently expressed Gγ subunit that might provide a membrane

anchor for the Gβγ dimer (Anderson and Botella, 2007). We re-assessed the subcellular

localization of the XLGs using Agrobacterium-mediated transient transformation in N.

benthamiana, as opposed to biolistic expression in Vicia faba guard cells (Ding et al., 2008). Our

assays indicate that the three XLGs have variable preferences for nuclear localization (Fig. 7, and

Supplemental Fig. S6). The extra-nuclear localization of all three proteins at the cell periphery is

consistent with the recent report of XLG localization at the plasma membrane (Maruta et al.,

2015). Our BiFC data show XLG heterotrimer localization is restricted to the cell periphery,

specifically at the plasma membrane (Fig. 5 and 6). However, in BiFC, the two tagged

interacting proteins are physically coupled by the irreversible association of the split-

fluoroprotein, and are not free to move independently. Therefore, we examined the influence of

untagged Gβγ dimers on XLG localization, choosing XLG3:mVenus as an example since it

reliably showed near-even localization in the cytosol and nucleus. When provided in excess,

untagged AGB1/AGG1 or AGB1/AGG2 dimers were able to sequester XLG3 at the plasma

membrane, in many cases rendering the nucleus devoid of XLG3 signal (Fig. 10). In the absence

of co-supplied Gβγ, the diverse localization patterns are also supported by our bioinformatic

analysis and residue substitution mutants, which show that XLG2 has a non-canonical NLS (Fig.

8), and XLG3 has both a classical NLS (Ding et al., 2008) and an unconventional NES (Fig. 9).

It is intriguing to speculate that, upon activation and dissociation from Gβγ, the XLGs may act to

directly transfer signal from the plasma membrane to the nucleus. This idea is lent credence by

interaction of XLG with Related To Vernalization 1 (RTV1), a DNA-binding protein with a

plant-specific B3-like DNA binding domain (Heo et al., 2012). RTV1 plays an important role in

flowering time control, likely by regulating floral integrator genes such as SOC1, and FT. XLG2-



21

RTV1 interaction occurs in the nucleus, and stimulates RTV1 chromatin-binding in ChIP assays

(Heo et al., 2012).

XLGs function in G protein-related phenotypes If XLGs function with Gβγ dimers in a Gα-like manner, XLG mutation should result in G protein

associated phenotypes. Some indicators that XLGs participate in AGB1-signaling are known (see

Table 1). Based on analysis of G protein phenotypes in the literature, we identified four other

agb1 phenotypes in which gpa1 mutants behaved like wild-type, displayed an opposite

phenotype to agb1, or had not been assigned. Salt, tunicamycin, and D-glucose are abiotic

stresses that agb1 mutants are hypersensitive to during post-germination development. In the

absence of similar phenotypes in gpa1 mutants, we examined the xlg mutants and identified

agb1-like phenotypes in the xlg triple mutant (Figures 11-14). Our results thereby indicate that

XLG1,2,3/AGB1/AGG1,2 heterotrimers play a role in suppressing responses to abiotic stress.

Salt has recently been implicated in stimulation of the UPR (Liu and Howell, 2010; Wang et al.,

2011), much as tunicamycin traditionally has been. Therefore, G proteins can be hypothesized to

function as suppressors of the UPR downstream of the convergence of different stimuli such as

salt and tunicamycin. Similarly, AGB1, AGG1 and AGG2, but not GPA1, have been implicated

in cell death and ROS production downstream of receptor-like kinases (RLKs) such as BAK1-

interacting receptor-like kinase 1 (BIR1), Flagellin-sensitive 2 (FLS2), EF-Tu receptor (EFR)

and Chitin elicitor receptor kinase 1 (CERK1) (Liu et al., 2013). Additionally, Respiratory burst

oxidase proteins D- and F- (AtRbohD-/AtRbohF-) mediated P. syringae resistance and ROS

production are dependent on AGB1, but not GPA1 (Torres et al., 2013), and an increased rate of

powdery mildew entry into epidermal cells was observed upon surface inoculation of agb1, but

not gpa1 mutant leaves (Lorek et al., 2013). Indeed, Maruta et al. (2015) demonstrated that

disruption of either XLG2 or AGB1 was able to suppress the cell death phenotype of bir1, and

resulted in impaired pathogen defense responses, including ROS production. These results

illustrate that G proteins modulate multiple cell death pathways, either suppressing (Warpeha et

al., 2008; Wei et al., 2008; Chen and Brandizzi, 2012; Colaneri et al., 2014; Yu and Assmann,

2015) or stimulating (Liu et al., 2013; Maruta et al., 2015) cell death in a stimuli-specific

manner. XLGs also function in developmental pathways. xlg mutants display increased primary

root growth (Ding et al., 2008), and increased root waving and skewing (Pandey et al., 2008),



22

both of which are also agb1 phenotypes (Chen et al., 2006; Pandey et al., 2008). We demonstrate

that XLGs are also involved in the development of aerial tissues, with xlg mutants exhibiting an

increase in stomatal density (Fig. 14).

The subunit phenotypes, including those summarized in Table 1, and those we analyzed in

Figures 11-14, correlate well with the heterotrimer configurations we observed in yeast (Fig. 1).

We found significant overlap of agg1 and agg2 phenotypes with xlg phenotypes. With the

exception of hypersensitivity to glucose during germination (Pandey et al., 2006; Trusov et al.,

2007), few overlapping phenotypes between gpa1 and agg1/agg2 mutants have been identified

to date. This observation, in combination with our yeast data, suggests that there are eight higher

affinity heterotrimer combinations: GPA1/AGB1/AGG3, XLG1/AGB1/AGG1,

XLG1/AGB1/AGG2, XLG2/AGB1/AGG1, XLG2/AGB1/AGG2, XLG3/AGB1/AGG1,

XLG3/AGB1/AGG2, and XLG3/AGB1/AGG3 that are responsible for the majority of G protein

signaling. Our criteria for choosing potential xlg phenotypes to investigate centered on agg1

and/or agg2 phenotypes that were not recapitulated in gpa1 mutants. Therefore, it should be

noted that our study was deliberately biased towards investigation of potential xlg/agb1/agg1-

agg2 phenotypes, and was not expected to identify additional gpa1/agb1/agg1-agg2 phenotypes.

The distinct phenotypes displayed by gpa1 and xlg mutants suggest that GPA1 and the XLGs

mediate distinct molecular pathways, at least in some cases, and that competition between GPA1

and the XLGs for Gβγ-binding could be important for molecular function. Additionally, GPA1

and the XLGs would be expected to bind and regulate different sets of effectors. A small number

of GPA1 interactors have been described which could be evaluated for interaction with XLGs,

including Phospholipase Dα1 (PLDα1) (Zhao and Wang, 2004), Prephenate Dehydratase 1

(PD1) (Warpeha et al., 2006), Pirin1 (PRN1) (Warpeha et al., 2007; Orozco-Nunnelly et al.,

2014), Thylakoid Formation1 (THF1) (Huang et al., 2006), and those identified in the

interactome of Klopffleisch et al. (2011). There may also be effector specificity within the XLG

family, as the majority of the G protein-related pathogen responses have been attributed to XLG2

(Zhu et al., 2009; Maruta et al., 2015). However, significant overlap among XLG effectors is

also expected, due to the redundancy displayed by the XLGs in our salinity (Fig. 11),

tunicamycin (Fig. 12), glucose (Fig. 13), and stomatal density (Fig. 14) assays.



23

Extending G protein heterotrimer diversity The lack of G protein diversity in plants such as Arabidopsis has been an unexpected finding in

the post-genomic era. Initial identification of GPA1, AGB1 (Gβ), and AGG1/AGG2 (Gγ),

allowed for only two different heterotrimer combinations, which was assumed from 2001 to

2011 to be the full complement of Arabidopsis G protein subunits, until the identification of the

atypical Gγ subunit, AGG3 (Chakravorty et al., 2011). Even characterization of AGG3 only

expanded the number of heterotrimer combinations to three, and surprisingly, suggested that Gγ

was the only subunit conferring isoform diversity in Arabidopsis. Here we provide evidence

from several complementary approaches that all three XLGs function as components of the

heterotrimeric G protein complex. XLGs and GPA1 bind selected Gβγ dimers with similar or

greater strength (Fig. 1), and XLG3 and GPA1 compete with each other for binding of

AGB1/AGG3 in our yeast results (Fig. 3). Furthermore, in silico analysis suggests that the three

XLG proteins structurally resemble GPA1 (Fig. 4, Supplemental Figs. S1 and S2, and

Supplemental Tables S1 and S2). All three XLGs interact with Gβγ dimers in planta (Fig. 5),

XLG3 is sequestered at the plasma membrane by both AGB1/AGG1 and AGB1/AGG2 (Fig. 10),

and xlg triple mutants phenocopy several agb1 phenotypes (Figs. 11-14). It therefore appears that

the Gα family in Arabidopsis comprises four members: GPA1, XLG1, XLG2 and XLG3. The

addition of the XLGs as Gα subunits expands the repertoire of heterotrimer combinations from

three to twelve.

Methods Plant Lines and Growth Conditions All T-DNA insertions used have been described previously and were isolated in the Col-0

background, with the exception of agg1-1c, which was identified in the WS ecotype but

introgressed into Col-0 by Trusov et al. (2007). Mutants used were: gpa1-3, gpa1-4 (Jones et al.,

2003), agb1-2 (Ullah et al., 2003), xlg1-1, xlg2-1, xlg3-1 and the xlg1-1 xlg2-1 xlg3-1 triple

mutant (Ding et al., 2008), agg1-1c, agg2-1 (Trusov et al., 2007), agg3-1 (Chakravorty et al.,

2011). Aside from the agg1-1c agg2-1 double mutant (Trusov et al., 2007), the Gγ double and

triple mutants have not previously been described, but are combinations of the above published



24

alleles. Arabidopsis plants were grown in Metro Mix 360 soil (Sun Gro Horticulture) and N.

benthamiana plants were grown in a 1:1 mix of Metro Mix 360: Sunshine Mix LC1 (Sun Gro

Horticulture), in growth chambers with 8-h light/16-h dark cycles, 120 µmol photons m-2 sec-1

light, and at 20°C.

Yeast 3-hybrid Experiments XLG clones were mobilized from pCR®8/GW/TOPO® (Life Technologies) into pDEST-GADT7

(Uetz et al., 2006) by Gateway cloning methods (Life Technologies). Gγ subunit genes and

truncations of the Gγ subunits were cloned into the EcoRI/SalI restriction sites of MCS1 of

pBridge. AGB1 was cloned into the NotI/BglII restriction sites of MCS2 to generate yeast 3-

hybrid constructs that express the Gβ and Gγ subunits. Competition assay constructs were made

by cloning XLG3 or GPA1 into the SpeI/EcoRI sites of p416GPD under control of the strong

yeast promoter GPD. The GPDpr::XLG3::CYC1 terminator, and GPDpr::GPA1::CYC1

terminator expression cassettes were excised from the vectors by PCR, which added flanking

NotI and BspEI restriction sites. The PCR fragments were cloned into the NotI/BspEI sites in the

backbone of pDEST-GADT7-GPA1 and pDEST-GADT7-XLG3 vectors, respectively, yielding

pDEST-GADT7-GPA1-GPDpr::XLG3 and pDEST-GADT7-XLG3-GPDpr::GPA1 vectors for

competition assays.

Yeast assays were performed in the Y2HGold yeast strain (Clontech). Diploid cells were selected

on SC-Trp-Leu plates. To test for the presence and strength of interactions, diploid cells were

spotted onto SC-Trp-Leu-Met-His media, supplemented with a range of 3-AT concentrations (0,

1, 2, 5, 10, 20 and 30 mM) to suppress histidine synthesis at increasing 3-AT levels (Durfee et

al., 1993). Interaction was assessed by activation of the histidine synthesis reporter gene, which

was scored by yeast growth, and strength of interaction was assessed by growth on plates

supplemented with progressively higher 3-AT concentrations.

BiFC and Fluorescent Protein Analyses BiFC and localization analysis was performed essentially as previously described (Gookin and

Assmann, 2014). Protocols for agroinfiltration, protoplast transformation, and confocal

microscopy, as well as description of the improved pDOE vector set used here, can be found in



25

Gookin and Assmann (2014). Cloning was performed using the strategies outlined in detail in

Gookin and Assmann (2014), Methods S1 and S2. Briefly, XLGL protein fusions with internal

NVen210 fragments were created by overlap PCR and inserted into the pDOE-10 MCS1

(simultaneously removing the vector encoded tag) to create parent vectors. AGB1 was inserted

into MCS3 to create the three Ubiquitin 10 promoter driven XLGL—CVen210:AGB1 test

vectors. Ubiquitin 10 driven XLG and residue substituted XLG:mVenus fusions were created

similarly by bridging pDOE-17 MCS1 and MCS3 in one cloning step (i.e. the 5’ end of the ORF

was cloned into MCS1 and the 3’ end into MCS3). Likewise, the mTq2:Histone 2B construct

was created by bridging MCS1 and MCS3 of pDOE-19. The 35S promoter driven untagged

AGB1-AGG and single AGG constructs were made similarly, and utilized previously (Gookin

and Assmann, 2014). Agroinfiltration at low optical densities (OD) is critical for avoiding

artifacts, therefore test vectors were infiltrated at a final OD600 of 0.00075-0.010. When utilized,

additional subunits were added in presumed excess, by infiltrating at an OD600 of 0.025-0.03.

The FM4-64 dye (Life Technologies), which marks the plasma membrane, was diluted to 50 µM

and infiltrated into the transiently transformed N. benthamiana leaves just prior to imaging.

Population level images were acquired at 20x magnification. Finer detail images were collected

using a 40x magnification water-immersion objective. High resolution/magnification images

showing the specificity of Histone 2B and XLG co-localization, and the specific overlap of

XLG-Gβγ heterotrimer formation with the plasma membrane marker dye FM4-64 were obtained

using a 63x oil-immersion lens and a 1.1 μm optical slice. The specific localization of XLG-Gβγ

heterotrimer formation at the plasma membrane was further demonstrated at 95x magnification

by the additional application of a 1.5x zoom of the confocal scan area during image acquisition

(0.09 μm/pixel resolution). Images were acquired using a Zeiss LSM-510 confocal microscope

and analyzed using the Zen 2009/2012 software.

Plate Assays Plate assays were performed on standard 0.5X MS media (Sigma) plates with 1% agar (Sigma),

supplemented with 1% sucrose (Calbiochem) for all assays except the glucose sensitivity assay.

After plating, seeds were stratified at 4°C for 2 days before plates were transferred to short day

growth chamber conditions, described above. Assays were performed with plates oriented

horizontally. In the salt sensitivity assay, seeds were plated as described above, and grown for



26

nine days, and then seedlings were transferred to media supplemented with 150 mM NaCl (EMD

Millipore). Seedlings were grown for an additional 14-21 days. Tunicamycin assays were

performed similarly to the assay of Wang et al. (2006). Briefly, seeds were initially plated on

media supplemented with 0.15 µM tunicamycin (Sigma). Seedlings were grown for six days,

transferred to standard media, and allowed to recover for an additional ten days before scoring.

Seedlings fell into three categories in our scoring system: 1) seedlings that did not grow after

transfer from the tunicamycin plates, and were clearly chlorotic and brown (dead); 2) seedlings

that grew and often greened after transfer but were visibly impaired in their growth (stunted); 3)

seedlings that thrived after transfer (healthy). Glucose sensitivity assays were performed using

media supplemented with 1-6% D-glucose (Sigma) instead of sucrose, with seedlings grown

under a long day 16-h light/8-h dark cycle. Seeds were germinated under high light conditions

(120 µmol photons m-2 sec-1) for one day, before lights were dimmed to 60 µmol photons m-2

sec-1 as per the method of Wang et al. (2006), who described their assay as run under “dim

light”. Seedlings were grown for 24 days. All plate assays were repeated at least three times with

similar results.

Stomatal density assay Seeds were plated and stratified as above. Seedlings were grown horizontally for nine days in

growth chambers with 8-h light/16-h dark cycles, 90 to 100 µmol photons m-2 sec-1 light, and at

20°C. Cotyledons were excised, stained with 1.5 μM propidium iodide (Sigma) for 30 min in the

dark, and mounted on cover slips with the abaxial side facing down. Images of abaxial epidermes

were taken using a Zeiss LSM-510 inverted confocal microscope with a 20x objective lens. At

least 10 seedlings were used for each genotype. Stomatal density was quantified from the

images.

Anthocyanin extraction Anthocyanins were extracted according to the method of Mancinelli et al. (1991), with minor

modifications. Briefly, intact aerial tissue of three to five seedlings was weighed, placed in acidic

methanol (1% HCl), and stored at 4°C in the dark overnight. Absorbance of the buffer with the

leached pigments was measured in duplicate at A530 and A657 for three independent samples per

genotype per condition, using a Nanodrop 2000 (Thermo Scientific). The peak absorbance of



27

anthocyanins occurs at 530 nm; however chlorophyll also absorbs light at 530 nm, at

approximately 25% of its peak absorbance at 657 nm. Therefore, as per the procedure of

Mancinelli et al. (1991), comparative anthocyanin content was estimated by calculating (A530 -

0.25 x A657) per mg of aerial tissue.

Supplemental Data

Figure S1. Predicted secondary structure elements of the Gα regions of the XLGs.

Figure S2. Rotated view of the predicted XLG3 structure in Figure 4.

Figure S3. ProSA validation of the XLG3 Gα theoretical structure model.

Figure S4. ERRAT analysis of the XLG3 Gα theoretical structure model.

Figure S5. Population level images of XLG-AGB1 BiFC.

Figure S6. High magnification co-localization of XLGs and Histone 2B.

Table S1. Summary of structural template matches for the XLG proteins, obtained using Phyre2.

Table S2. Summary of structural template matches for the XLG proteins, obtained using

genTHREADER.

Supplemental File 1. PDB file of the computationally derived XLG3alpha structure.



28

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Figure Legends Figure 1. Y3H assays demonstrate specificity of GPA1 for AGB1/AGG3, XLG1 and XLG2 for AGB1/AGG1 and AGB1/AGG2, and XLG3 for all three Gβγ dimers. Yeast 3-hybrid

assays testing interactions between (A) GPA1, (B) XLG1, (C) XLG2, and (D) XLG3 (GAL4

activation domain fusions), with the AGB1/AGG1 (Gβγ1), AGB1/AGG2 (Gβγ2) and

AGB1/AGG3 (Gβγ3) Gβγ dimers (Gγ fused to the GAL4 binding domain, Gβ (AGB1) as the

bridge protein). A truncated “γ3(γ)” was also tested, consisting of only the Gγ-like domain of

AGG3 (residues 1-112), lacking the implicated transmembrane domain. Yeast growth on SC-

Trp-Leu (Growth) confirmed transformation and cell viability. Interactions were assayed on SC-

Trp-Leu-Met-His, supplemented with the indicated concentrations of 3-AT (0 to 30 mM).

Figure 2. The interaction of XLGs with Gγ subunits is AGB1-dependent. Yeast 3-hybrid

assays testing interactions of GPA1, XLG1, XLG2, and XLG3 with the AGG1 (Gγ1), AGG2

(Gγ2) and AGG3 (Gγ3) subunits. Interactions were assayed in the presence and absence of

AGB1. A truncated “γ3(γ)” subunit was also included, which includes only the Gγ-like domain

of AGG3 (residues 1-112). All interactions were assayed by growth on SC-Trp-Leu-Met-His

supplemented with 2 mM 3-AT. Two mM 3-AT was used because the pBridge-AGG1 construct

exhibited autoactivation (i.e., growth in combination with the empty vector) on SC-Trp-Leu-

Met-His supplemented with 0 or 1 mM 3-AT.

Figure 3. GPA1 and XLG3 compete with each other for binding of AGB1/AGG3 in yeast. Yeast 3-hybrid competition assays, testing the interaction between GPA1 and AGB1/AGG3(γ)

(Gβγ3(γ)) with or without additional expression of XLG3, and the interaction between XLG3

and AGB1/AGG3(γ) (“Gβγ3(γ)”) with or without additional expression of GPA1. The fourth

protein (XLG3 or GPA1, respectively) was expressed under the control of the strong GPD

promoter. All interactions were assayed by growth on SC-Trp-Leu-Met-His, supplemented with

2 mM 3-AT.

Figure 4. The XLG3 Gα-like region aligns closely to the crystal structure of GPA1.

Superimposition of computationally derived XLG3 structural features on the empirically derived



36

GPA1 crystal structure demonstrates their shared 3-D characteristics. Blue = XLG3 Gα-like

region, orange = GPA1 Gα-like region, N = amino terminus of the Gα regions. Thr-132 marks

the NVen210 insertion site in the αB-αC loop of GPA1 used for BiFC (Gookin and Assmann,

2014): each of the XLGs was modified at the analogous residue.

Figure 5. XLG1, XLG2 and XLG3 interact with AGB1 at the plasma membrane in an AGG dependent manner. In all assays, positive transformation is confirmed by Golgi-localized

mTurquoise2 fluorescence from the XT-Golgi-mTq2 marker. (A) The XLG1L—CVen210 parent

vector does not produce non-specific BiFC signal. (B) The XLG1L—CVen210:AGB1 construct

shows zero to near-zero signal in the absence of a co-expressed Gγ subunit. (C) The XLG1L—

CVen210:AGB1 construct produces BiFC signal in the presence of co-expressed AGG1. (D) The

XLG1L—CVen210:AGB1 construct produces BiFC signal in the presence of co-expressed

AGG2. (E) The XLG1L—CVen210:AGB1 construct produces BiFC signal in the presence of

co-expressed AGG3. (F) The XLG2L—CVen210 parent vector does not produce non-specific

BiFC signal. (G) The XLG2L—CVen210:AGB1 construct shows zero to near-zero signal in the

absence of a co-expressed Gγ subunit. (H) The XLG2L—CVen210:AGB1 construct produces

BiFC signal in the presence of co-expressed AGG1. (I) The XLG2L—CVen210:AGB1 construct

produces BiFC signal in the presence of co-expressed AGG2. (J) The XLG2L—CVen210:AGB1

construct produces BiFC signal in the presence of co-expressed AGG3. (K) The XLG3L—

CVen210 parent vector does not produce non-specific BiFC signal. (L) The XLG3L—

CVen210:AGB1 construct shows zero to near-zero signal in the absence of a co-expressed Gγ

subunit. (M) The XLG3L—CVen210:AGB1 construct produces BiFC signal in the presence of

co-expressed AGG1. (N) The XLG3L—CVen210:AGB1 construct produces BiFC signal in the

presence of co-expressed AGG2. (O) The XLG3L—CVen210:AGB1 construct produces BiFC

signal in the presence of co-expressed AGG3. Parent vectors were agroinfiltrated into N.

benthamiana leaves at OD600 of 0.0075-0.010 and images were acquired 57-60 hrs post-

infiltration. Yellow = mVenus BiFC, blue = mTurquoise2, red = chlorophyll autofluorescence.

Scale bars = 50 μm.

Figure 6. XLG-based heterotrimers localize specifically to FM4-64 marked plasma membranes. The ubiquitin10 promoter driven XLG–AGB1 test constructs were co-transformed



37

with the 35S driven pDOE-γ1γ2 vector (Gookin and Assmann, 2014) as a source of untagged

AGG1 and AGG2. (A) XLG1 interacts with AGB1. (B) FM4-64 stains the plasma membrane.

(C) XLG1-AGB1 BiFC signal overlaps with the FM4-64 marked plasma membrane. (D) XLG2

interacts with AGB1. The four white arrows mark the plasma membranes of two adjacent

transformed cells traversing in and out of the 1.1 μm focal plane. (E) FM4-64 marks the plasma

membrane. (F) XLG2-AGB1 BiFC signal overlaps with the FM4-64 marked plasma membrane.

(G) XLG3 interacts with AGB1. (H) FM4-64 stains the plasma membrane. (I) XLG3-AGB1

BiFC signal overlaps with the FM4-64 marked plasma membrane. (J) High

resolution/magnification image of the XLG3-AGB1 BiFC signal visible at the two distinct

plasma membranes of two adjacent cells, marked with white arrows. (K) FM4-64 specifically

labels the two distinct plasma membranes. White arrows mark FM4-64 labeled vesicles. (L)

XLG3-AGB1 BiFC signal overlaps with the two distinct FM4-64 marked plasma membranes,

but not with the FM4-64 marked vesicles. Test vectors were agroinfiltrated into N. benthamiana

leaves at OD600 of 0.0075 and images were acquired 62-67 hrs post-infiltration. FM4-64 was

infiltrated at 50 μM just prior to imaging. Images in A-I were acquired at 63x magnification with

a 1.1 μm optical slice, scale bars = 20 μm. Images in J-L were acquired at 95x (63x

magnification plus a 1.5 zoom of the scan area during image acquisition, 0.09 μm/pixel

resolution), scale bars = 5 μm. Yellow = mVenus BiFC, red = FM4-64.

Figure 7. Subcellular localization of Arabidopsis XLG proteins in N. benthamiana leaves. Ubiquitin 10 promoter driven XLG:mVenus fusions show differing localization patterns. XLG1

is predominately extra-nuclear with (A) nearly undetectable to (B) very weak nuclear signal.

XLG2 varies between (C) strong nuclear and (D) evenly divided between the nucleus and

cytoplasm. (E and F) XLG3 consistently localizes to the nucleus and the cytoplasm.

Agroinfiltrations of N. benthamiana leaves were performed at an OD600 of 0.0075-0.010 and

imaged at 60-68 hrs, except for (F) imaged 6 days post-infiltration. Yellow = mVenus, blue =

mTurquoise2, red = chlorophyll autofluorescence. Scale bars = 50 μm.

Figure 8. XLG2 has a functional nuclear localization signal. (A) The XLG2 NLS has a

similar basic-positive patch of residues (red) and a CAVF motif (blue) identical to the

empirically validated Clone a6 sequence (Kosugi et al., 2009). (B) The XLG2 NLS resides in a



38

semi-conserved stretch of sequence in the XLG family starting at XLG2 residue 424, and the

arrows show the XLG1 residues mutated to mirror XLG2 to create the XLG1m1 construct.

XLG1m1:mVenus fusions localized to the nucleus in N. benthamiana leaves, demonstrating that

the XLG2 NLS is a functional regulatory domain. (Compare to XLG1:mVenus localization in

Figure 7, A and B.) (C to F) Agroinfiltration of XLG1m1:mVenus into N. benthamiana leaves at

OD600 of 0.0075-0.010 and imaged 48 hr later at 63x magnification. (C) XLG1m1:mVenus

localizes to the interior of the nucleus and at the plasma membrane; the nucleolus (white arrow)

does not appreciably accrue XLG1m1. (D) The nucleus is specifically marked by mTq2:Histone

2B. (E) The nucleus and nucleolus (white arrow) are clearly visible in the brightfield channel. (F)

XLG1m1:mVenus and mTq2:Histone 2B co-localization is specific to the nucleus. Yellow =

mVenus, blue = mTurquoise2, red = chlorophyll autofluorescence. Scale bar = 10 μm.

Figure 9. XLG3 has a functional nuclear export signal. (A) The N-terminal domain of XLG3

has an unconventional NES (triangle) located just upstream of the Gα like region. The XLG3

NES was mutated by substituting hydrophobic residues at the N-terminus (XLG3m1) or the C-

terminus (XLG3m2) of the domain with glycines. Both mutants showed near exclusive nuclear

localization. (B and C) XLG3m1 nuclear localization in two focal planes of the same mesophyll

cells. (D) XLG3m2 nuclear localization in epidermal pavement cells. Agroinfiltrations of N.

benthamiana leaves were performed at an OD600 of 0.0075-0.010 and imaged 50-55 hr later.

Yellow = mVenus, blue = mTurquoise2, red = chlorophyll autofluorescence. Scale bar = 50 μm

Figure 10. Overexpression of Gβγ dimers sequesters XLG3 at the plasma membrane. XLG3::mVenus driven by the UBQ10 promoter is retained at the plasma membrane when co-

expressed with 35S driven (A) AGB1-AGG1 or (B) AGB1-AGG2 dimers. (Compare with

localization of the XLG3::mVenus fusion protein in the absence of additional Gβγ in Figure 7, E

and F.) Note the lack of nuclear signal in two nuclei (white arrows) visible in the brightfield

channel. The plasma membrane retention was consistent over time; the images above were

acquired 6 days post-infiltration of N. benthamiana leaves at a final OD600 of 0.0075 for XLG3,

and 0.025 for Gβγ dimers. Yellow = mVenus, blue = mTurquoise2, red = chlorophyll

autofluorescence. Scale bars = 50 μm.



39

Figure 11. agb1, agg1 agg2 and the xlg triple mutants are hypersensitive to salt. Seeds were

sown and germinated on 0.5X MS plates (1% sucrose and 1% agar). After 9 days of growth,

seedlings were transferred to 0.5X MS plates (1% sucrose and 1% agar) supplemented with 150

mM NaCl. Seedling survival was scored once seedling death was apparent in the most severely

affected genotypes (14-21 days). Assays were conducted with (A) mutants of the Gγ subunits,

and (B and C) xlg mutants. A representative image of the results with the xlg mutants and agb1-2

is shown in (B) and quantification is shown in (C). Col-0, agb1 and gpa1 controls were included

in both assays. In (B), ‘xlg triple’ refers to the xlg1-1 xlg2-1 xlg3-1 mutant. Significant

differences from Col-0 (Student’s t-test) are indicated (*P < 0.05–0.01; **P < 0.01–0.001; ***P

< 0.001). All values are mean ± SE.

Figure 12. agb1, agg1 agg2 and the xlg triple mutants are hypersensitive to tunicamycin. Seeds were sown and germinated on 0.5X MS plates (1% sucrose and 1% agar) supplemented

with 0.15 µM tunicamycin. After 6 days of growth, seedlings were transferred to 0.5X MS plates

(1% sucrose and 1% agar) and allowed to recover for an additional ten days before being scored,

as outlined in the Materials and Methods. Seedlings that failed to thrive (stunted + dead

seedlings) are presented for: (A) mutants of the Gγ subunits, and (B and C) xlg mutants. A

representative image of the results with the xlg mutants and agb1-2 is shown in (B) and

quantification is shown in (C). Col-0, agb1 and gpa1 controls were included in both assays. In

(B), ‘xlg triple’ refers to the xlg1-1 xlg2-1 xlg3-1 mutant. Significant differences from Col-0

(Student’s t-test) are indicated (*P < 0.05–0.01; **P < 0.01–0.001; ***P < 0.001). All values are

mean ± SE.

Figure 13. agb1, agg1 and the xlg triple mutants are hypersensitive to D-glucose. Seeds were

sown on 0.5X MS plates (1% agar) supplemented with 1 or 6% D-glucose. Seeds were

germinated under 120 µmol m-2 sec-1 white light for 1 day, then light intensity was dimmed to 60

µmol m-2 sec-1. After 24 days of growth in long day conditions, anthocyanins were extracted and

quantified for: (A) mutants of the Gγ subunits, and (B) xlg mutants. Col-0, agb1 and gpa1

controls were included in both assays. Significant differences from Col-0 (Student’s t-test) are

indicated (*P < 0.05–0.01; **P < 0.01–0.001; ***P < 0.001). All values are mean ± SE.



40

Figure 14. agb1, agg1 agg2 and the xlg triple mutants display increased stomatal density. Propidium iodide stained cotyledons of nine-day-old seedlings were imaged using a confocal

microscope, and images were used to quantify stomatal density for; (A) mutants of the Gγ

subunits, and (B) xlg mutants. Representative images of propidium iodide stained cotyledons are

shown for (C) Col-0, (D) gpa1-4, (E) agb1-2, and (F) the xlg triple mutant. White = propidium

iodide stain. Scale bars = 50 µm. The assay was conducted for all genotypes simultaneously, and

the Col-0, agb1-2 and gpa1-3 controls represent the same data in (A) and (B). Significant

differences from Col-0 (Student’s t-test) are indicated (*P < 0.05–0.01; **P < 0.01–0.001; ***P

< 0.001). All values are mean ± SE.

Table 1. Summary of phenotypic differences between gpa1 and agb1 mutants, and participation of the XLGs in these phenotypes. G protein phenotypes from the literature in

which gpa1 and agb1 mutants display opposite or different phenotypes are listed. Phenotypes of

gpa1, agb1, xlg, agg1/agg2, and agg3 mutants are annotated as hypersensitive, hyposensitive or

WT (wild-type) for responses. Morphological phenotypes are annotated as increased, decreased

or WT. New results from this article are included in bold. Phenotypes were often found to be

similar or aligned between xlg, agb1, and agg1/agg2 mutants.



41

Supplemental Figure Legends

Figure S1. Predicted secondary structure elements of the Gα regions of the XLGs match closely with those of GPA1. Helical (green) and strand (blue) secondary structures, as predicted

by Phyre2, superimposed on a Clustal omega alignment of GPA1 and the Gα regions of XLG1

(residues 446 to 888), XLG2 (residues 435 to 861) and XLG3 (residues 396 to 848). Gaps in the

alignment were manually adjusted to minimize disruption of predicted structural elements. The

initial native residue of the empirically derived GPA1 crystal structure (PDB:2XTZ) (Jones et

al., 2011a), and our computationally derived XLG3 structural model (Figure 4 and Supplemental

Figure S2), are indicated with a red arrow. Note: an exogenous MSGI tetrapeptide is located at

the N-terminus of the GPA1 crystal structure, and is computationally added in our XLG3

structural model. Therefore, the first native residue corresponds to residue number 5 in both

structures.

Figure S2. An alternative view of the XLG3-GPA1 Gα-like region superimposition. The

XLG3alpha.pdb-2XTZ structural superimposition shown in main text Figure 4 was horizontally

rotated 145 degrees for visualization of the other side of the structure, and to illustrate the

position of the αB-αC loop position (Thr-132 of GPA1) used to insert NVen210 into the G

proteins. Blue = XLG3 Gα-like region, orange = GPA1 Gα-like region, N = amino terminus of

the Gα regions.

Figure S3. ProSA validation of the XLG3 Gα domain theoretical structure. The

XLG3alpha.pdb structure prediction (I-TASSER model.1) was analyzed using the ProSA-web

server available at https://www.came.sbg.ac.at/prosa.php. (A) The overall quality of the

predicted XLG3 Gα domain structure localizes near the middle of a plot for all experimentally

derived protein structures. The black dot at coordinates (424, -7.2) specifically identifies the

location of the XLG3alpha.pdb structure in the plot. (B) The ProSA local quality analysis with a

moving window size of 40 shows the XLG3alpha.pdb model only has two potentially

problematic segments (positive values).



42

Figure S4. ERRAT analysis of the XLG3 Gα domain theoretical structure. Stringent

analysis of the XLG3alpha.pdb structure prediction (I-TASSER model.1) using ERRAT, which

is designed to evaluate actual crystal structures, shows the predictive model generally passes as a

plausible protein structure. ERRAT identifies several segments where the exact placement of

amino acids may not be replicated in an empirically resolved XLG3 crystal structure. ERRAT

was run using The Structure Analysis and Verification Server web service, available at

http://services.mbi.ucla.edu/SAVES/.

Figure S5. Population level images showing XLGs interact with AGB1 in an AGG dependent manner. In all assays, positive transformation is confirmed by the XT-Golgi-mTq2

marker which specifically labels Golgi. (A) The XLG1L—CVen210:AGB1, (E) XLG2L—

CVen210:AGB1, and (I) XLG3L—CVen210:AGB1 test vectors produce zero to near zero BiFC

signal without the addition of exogenous Gγ subunits. Positive BiFC signal is produced when

XLG1L—CVen210:AGB1 is co-expressed with (B) AGG1, (C) AGG2, and (D) AGG3. Positive

BiFC signal is observed when XLG2L—CVen210:AGB1 is co-expressed with (F) AGG1, (G)

AGG2, and (H) AGG3. Positive BiFC signal is produced by XLG3L—CVen210:AGB1 with co-

expressed (J) AGG1, (K) AGG2, and (L) AGG3. Yellow = mVenus BiFC, blue = mTurquoise2,

red = chlorophyll autofluorescence. Scale bars = 100 μm.

Figure S6. Confirmation of XLG subcellular localization using Histone 2B as a nuclear marker. Ubiquitin10 driven XLG:mVenus fusions show differential nuclear localization, as

confirmed by co-localization with mTq2 tagged Histone 2B. (A) XLG1 is predominantly non-

nuclear even at 72 hrs post-infiltration. (B) Histone 2B specifically marks the nucleus. (C)

Overlap image of XLG1 and Histone 2B. (D) XLG2 localizes to the plasma membrane and the

nucleus at 72 hrs post-infiltration. (E) Histone 2B specifically marks the nucleus. (F) The XLG2

and Histone 2B signals overlap in the nucleus. (G) XLG3 localizes to the plasma membrane and

the nucleus. Note two nuclei are visible. (H) Histone 2B specifically marks two nuclei. (I) XLG3

and Histone 2B signals overlap in the nuclei. Images were acquired with a 63x oil-immersion

objective. Yellow = mVenus, blue = mTq2 (mTurquoise), red = chlorophyll autofluorescence,

scale bars = 20 μm.



43

Table S1. XLG proteins are matched with Gα subunit structural templates by Phyre2. Table of the top 20 hits from the protein fold library in the Phyre2 database (based on PDB

structures) which matched to each of the XLG1, XLG2 and XLG3 protein sequences. Fold

library entries in the Phyre2 database use identifiers that start with a ‘C’ for chain, or ‘D’ for

domain, then include the PDB structure identifier, and end with the chain code from the PDB

structure. For clarity we present the PDB identifier underlined within the fold library identifier.

All of the top 20 structural templates that Phyre2 matched to each XLG correspond to Gα

proteins, or fragments thereof, with confidence levels of 99.9 to 100%. In the table, hits were

sorted into chain vs. domain folds, then by confidence level and % ID assigned by Phyre2, first

by XLG1 scores, then XLG2 and XLG3. The structural template corresponding to the GPA1

crystal structure (PDB:2XTZ) (Jones et al., 2011a) is identified by Phyre2 as C2XTZB and is in

bold.

Table S2. XLG proteins are matched with Gα subunit structural templates by genTHREADER. Table of the hits from the genTHREADER structure library (based on PDB

structures) which matched to each of the XLG1, XLG2 and XLG3 protein sequences as ‘certain’

(p-value <0.0001) or ‘high’ (p-value 0.0001-0.001). Structure library entries in the

genTHREADER database use identifiers that start with the PDB structure identifier, followed by

the chain code from the PDB structure. For clarity we present the PDB identifier underlined. The

13 structural templates that genTHREADER matched to each of the XLGs as ‘certain’ or ‘high’

correspond to the same 13 Gα proteins. Hits were sorted by score of their match with XLG1. The

structural template corresponding to the GPA1 crystal structure (PDB:2XTZ) (Jones et al.,

2011a) is identified by genTHREADER and is in bold.



44

Table 1. Summary of phenotypic differences between gpa1 and agb1 mutants, and participation of the XLGs in these phenotypes. G protein phenotypes from the literature in

which gpa1 and agb1 mutants display opposite or different phenotypes are listed. Phenotypes of

gpa1, agb1, xlg, agg1/agg2, and agg3 mutants are annotated as hypersensitive, hyposensitive or

WT (wild-type) for responses. Morphological phenotypes are annotated as increased, decreased

or WT. New results from this article are included in bold. Phenotypes were often found to be

similar or aligned between xlg, agb1, and agg1/agg2 mutants.

Phenotype Genotypes gpa1 agb1 xlgs agg1/2 agg3

Susceptibility to pathogens

↓ Decreased [1,2]

↑ Increased [1,2,3,4]

↑ Increased [3,4]

↑ Increased [5]

─ WT [6]

Primary root growth rate/length

─ WT [7,8]

↑ Increased [7,8]

↑ Increased [7]

─ WT [9]

Lateral root proliferation

↓ Decreased [10]

↑ Increased [10]

↑ Increased [7]

↑ Increased [5]

─ WT [6]

Root waving and skewing

↓ WT/minor decrease [11]

↓ Decreased [11]

↓ Decreased [11]

Sensitivity to salt post-germination

↓ Hyposensitive [12]

↑ Hypersensitive [12]

↑ Hypersensitive

↑ Hypersensitive

─ WT

Sensitivity to tunicamycin post-germination

─ WT

↑ Hypersensitivea [13]

↑ Hypersensitive

↑ Hypersensitive

─ WT

Sensitivity to D-glucose post-germination

─ WT

↑ Hypersensitive [14]

↑ Hypersensitive

↑ Hypersensitive

─ WT

Stomatal density/index ↓

Decreased [15,16] ↑

Increased [15] ↑

Increased ↑

Increased ─

WT [6] aWang et al. (2007) described the opposite with agb1 hyposensitive.

[1] Llorente et al. (2005), [2] Trusov et al. (2006), [3] Zhu et al. (2009), [4] Maruta et al. (2015),

[5] Trusov et al. (2007), [6] Chakravorty et al. (2011), [7] Ding et al. (2008), [8] Chen et al.

(2006), [9] Li et al. (2012), [10] Ullah et al. (2003), [11] Pandey et al. (2008), [12] Colaneri et al.

(2014), [13] Chen and Brandizzi (2012), [14] Wang et al. (2006), [15] Zhang et al. (2008), [16]

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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Trends Plant Sci%5BTitle%5D%29 AND 17%5BVolume%5D AND 563%5BPagination%5D AND Botella JR%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=The Heterotrimeric G-protein Complex Modulates Light Sensitivity in Arabidopsis thaliana Seed Germination&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Botto&as_ylo=2009&as_allsubj=all&hl=en&c2coff=1

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Choudhury SR, Bisht NC, Thompson R, Todorov O, Pandey S (2011) Conventional and Novel G? Protein Families Constitute theHeterotrimeric G-Protein Signaling Network in Soybean. PLoS One 6: e23361


Colaneri AC, Tunc-Ozdemir M, Huang JP, Jones AM (2014) Growth attenuation under saline stress is mediated by theheterotrimeric G protein complex. BMC Plant Biol. 14: 129


Colovos C, Yeates TO (1993) Verification of protein structures: Patterns of nonbonded atomic interactions. Protein Sci. 2: 1511-1519


Coursol S, Fan LM, Le Stunff H, Spiegel S, Gilroy S, Assmann SM (2003) Sphingolipid signalling in Arabidopsis guard cells involvesheterotrimeric G proteins. Nature 423: 651-654


Delgado-Cerezo M, Sanchez-Rodriguez C, Escudero V, Miedes E, Fernandez PV, Jorda L, Hernandez-Blanco C, Sanchez-Vallet A,Bednarek P, Schulze-Lefert P, Somerville S, Estevez JM, Persson S, Molina A (2012) Arabidopsis Heterotrimeric G-proteinRegulates Cell Wall Defense and Resistance to Necrotrophic Fungi. Mol. Plant. 5: 98-114


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Eisenberg D, Luthy R, Bowie JU (1997) VERIFY3D: Assessment of Protein Models with Three-Dimensional Profiles. In CW Carter,RM Sweet, eds, Macromolecular Crystallography, Pt B, Vol 277, pp 396-404


Fan LM, Zhang W, Chen JG, Taylor JP, Jones AM, Assmann SM (2008) Abscisic acid regulation of guard-cell K+ and anion channelsin G?- and RGS-deficient Arabidopsis lines. Proc. Natl. Acad. Sci. U. S. A. 105: 8476-8481


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http://scholar.google.com/scholar?as_q=Pathogen-secreted proteases activate a novel plant immune pathway.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Cheng&as_ylo=2015&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Conventional and Novel G%3F Protein Families Constitute the Heterotrimeric G%2DProtein Signaling Network in Soybean%2E%5BTitle%5D%29 AND Choudhury SR%2C Bisht NC%2C Thompson R%2C Todorov O%2C Pandey S%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Choudhury&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Conventional and Novel G? Protein Families Constitute the Heterotrimeric G-Protein Signaling Network in Soybean.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Conventional and Novel G? Protein Families Constitute the Heterotrimeric G-Protein Signaling Network in Soybean.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Choudhury&as_ylo=2011&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Growth attenuation under saline stress is mediated by the heterotrimeric G protein complex%2E%5BTitle%5D%29 AND Colaneri AC%2C Tunc%2DOzdemir M%2C Huang JP%2C Jones AM%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=Growth attenuation under saline stress is mediated by the heterotrimeric G protein complex.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Growth attenuation under saline stress is mediated by the heterotrimeric G protein complex.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Colaneri&as_ylo=2014&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Protein Sci%5BTitle%5D%29 AND 2%5BVolume%5D AND 1511%5BPagination%5D AND Colovos C%2C Yeates TO%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Colovos&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Verification of protein structures: Patterns of nonbonded atomic interactions&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Verification of protein structures: Patterns of nonbonded atomic interactions&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Colovos&as_ylo=1993&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Nature%5BTitle%5D%29 AND 423%5BVolume%5D AND 651%5BPagination%5D AND Coursol S%2C Fan LM%2C Le Stunff H%2C Spiegel S%2C Gilroy S%2C Assmann SM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Coursol S, Fan LM, Le Stunff H, Spiegel S, Gilroy S, Assmann SM (2003) Sphingolipid signalling in Arabidopsis guard cells involves heterotrimeric G proteins. Nature 423: 651-654

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http://scholar.google.com/scholar?as_q=Sphingolipid signalling in Arabidopsis guard cells involves heterotrimeric G proteins&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Sphingolipid signalling in Arabidopsis guard cells involves heterotrimeric G proteins&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Coursol&as_ylo=2003&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Mol%2E Plant%5BTitle%5D%29 AND 5%5BVolume%5D AND 98%5BPagination%5D AND Delgado%2DCerezo M%2C Sanchez%2DRodriguez C%2C Escudero V%2C Miedes E%2C Fernandez PV%2C Jorda L%2C Hernandez%2DBlanco C%2C Sanchez%2DVallet A%2C Bednarek P%2C Schulze%2DLefert P%2C Somerville S%2C Estevez JM%2C Persson S%2C Molina A%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Delgado-Cerezo M, Sanchez-Rodriguez C, Escudero V, Miedes E, Fernandez PV, Jorda L, Hernandez-Blanco C, Sanchez-Vallet A, Bednarek P, Schulze-Lefert P, Somerville S, Estevez JM, Persson S, Molina A (2012) Arabidopsis Heterotrimeric G-protein Regulates Cell Wall Defense and Resistance to Necrotrophic Fungi. Mol. Plant. 5: 98-114

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http://scholar.google.com/scholar?as_q=Arabidopsis Heterotrimeric G-protein Regulates Cell Wall Defense and Resistance to Necrotrophic Fungi&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Delgado-Cerezo&as_ylo=2012&as_allsubj=all&hl=en&c2coff=1

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Ding&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Arabidopsis extra-large G proteins (XLGs) regulate root morphogenesis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Arabidopsis extra-large G proteins (XLGs) regulate root morphogenesis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ding&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Genes Dev%5BTitle%5D%29 AND 7%5BVolume%5D AND 555%5BPagination%5D AND Durfee T%2C Becherer K%2C Chen PL%2C Yeh SH%2C Yang YZ%2C Kilburn AE%2C Lee WH%2C Elledge SJ%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Durfee&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Durfee&as_ylo=1993&as_allsubj=all&hl=en&c2coff=1

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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant J%5BTitle%5D%29 AND 80%5BVolume%5D AND 553%5BPagination%5D AND Gookin TE%2C Assmann SM%5BAuthor%5D&dopt=abstract

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Huang J, Taylor JP, Chen JG, Uhrig JF, Schnell DJ, Nakagawa T, Korth KL, Jones AM (2006) The Plastid Protein THYLAKOIDFORMATION1 and the Plasma Membrane G-Protein GPA1 Interact in a Novel Sugar-Signaling Mechanism in Arabidopsis. PlantCell 18: 1226-1238


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Ishida T, Tabata R, Yamada M, Aida M, Mitsumasu K, Fujiwara M, Yamaguchi K, Shigenobu S, Higuchi M, Tsuji H, Shimamoto K,Hasebe M, Fukuda H, Sawa S (2014) Heterotrimeric G proteins control stem cell proliferation through CLAVATA signaling inArabidopsis. EMBO Rep. 15: 1202-1209


Ishikawa A, Iwasaki Y, Asahi T (1996) Molecular Cloning and Characterization of a cDNA for the ? Subunit of a G Protein from Rice.Plant Cell Physiol. 37: 223-228


Ishikawa A, Tsubouchi H, Iwasaki Y, Asahi T (1995) Molecular Cloning and Characterization of a cDNA for the ??Subunit of a G-Protein from Rice. Plant Cell Physiol. 36: 353-359


Johnston CA, Taylor JP, Gao Y, Kimple AJ, Grigston JC, Chen JG, Siderovski DP, Jones AM, Willard FS (2007) GTPaseacceleration as the rate-limiting step in Arabidopsis G protein-coupled sugar signaling. Proc. Natl. Acad. Sci. U. S. A. 104: 17317-17322


Johnston CA, Willard MD, Kimple AJ, Siderovski DP, Willard FS (2008) A sweet cycle for Arabidopsis G-proteins: Recentdiscoveries and controversies in plant G-protein signal transduction. Plant Signaling & Behavior 3: 1067-1076


Jones AM, Ecker JR, Chen J-G (2003) A Reevaluation of the Role of the Heterotrimeric G Protein in Coupling Light Responses inArabidopsis. Plant Physiol. 131: 1623-1627


Jones DT (1999a) GenTHREADER: An Efficient and Reliable Protein Fold Recognition Method for Genomic Sequences. J. Mol.Biol. 287: 797-815


Jones DT (1999b) Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292: 195-202Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Jones JC, Duffy JW, Machius M, Temple BRS, Dohlman HG, Jones AM (2011a) The Crystal Structure of a Self-Activating G Protein? Subunit Reveals Its Distinct Mechanism of Signal Initiation. Sci. Signal. 4: ra8


Jones JC, Temple BRS, Jones AM, Dohlman HG (2011b) Functional Reconstitution of an Atypical G Protein Heterotrimer andRegulator of G Protein Signaling Protein (RGS1) from Arabidopsis thaliana. J. Biol. Chem. 286: 13143-13150


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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant Cell%5BTitle%5D%29 AND 18%5BVolume%5D AND 1226%5BPagination%5D AND Huang J%2C Taylor JP%2C Chen JG%2C Uhrig JF%2C Schnell DJ%2C Nakagawa T%2C Korth KL%2C Jones AM%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Huang&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The Plastid Protein THYLAKOID FORMATION1 and the Plasma Membrane G-Protein GPA1 Interact in a Novel Sugar-Signaling Mechanism in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The Plastid Protein THYLAKOID FORMATION1 and the Plasma Membrane G-Protein GPA1 Interact in a Novel Sugar-Signaling Mechanism in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Huang&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28and %3F Subunit Genes%2E DNA Res%5BTitle%5D%29 AND 7%5BVolume%5D AND 111%5BPagination%5D AND Hurowitz EH%2C Melnyk JM%2C Chen Y%2C Kouros%2DMehr H%2C Simon MI%2C Shizuya H%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Hurowitz EH, Melnyk JM, Chen Y, Kouros-Mehr H, Simon MI, Shizuya H (2000) Genomic Characterization of the Human Heterotrimeric G Protein ?, ?, and ? Subunit Genes. DNA Res. 7: 111-120

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Hurowitz&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Genomic Characterization of the Human Heterotrimeric G Protein&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Genomic Characterization of the Human Heterotrimeric G Protein&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Hurowitz&as_ylo=2000&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28EMBO Rep%5BTitle%5D%29 AND 15%5BVolume%5D AND 1202%5BPagination%5D AND Ishida T%2C Tabata R%2C Yamada M%2C Aida M%2C Mitsumasu K%2C Fujiwara M%2C Yamaguchi K%2C Shigenobu S%2C Higuchi M%2C Tsuji H%2C Shimamoto K%2C Hasebe M%2C Fukuda H%2C Sawa S%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Ishida&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Heterotrimeric G proteins control stem cell proliferation through CLAVATA signaling in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Heterotrimeric G proteins control stem cell proliferation through CLAVATA signaling in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ishida&as_ylo=2014&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Subunit of a G Protein from Rice%2E Plant Cell Physiol%5BTitle%5D%29 AND 37%5BVolume%5D AND 223%5BPagination%5D AND Ishikawa A%2C Iwasaki Y%2C Asahi T%5BAuthor%5D&dopt=abstract

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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Proc%2E Natl%2E Acad%2E Sci%2E U%2E S%2E A%5BTitle%5D%29 AND 104%5BVolume%5D AND 17317%5BPagination%5D AND Johnston CA%2C Taylor JP%2C Gao Y%2C Kimple AJ%2C Grigston JC%2C Chen JG%2C Siderovski DP%2C Jones AM%2C Willard FS%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=A sweet cycle for Arabidopsis G-proteins: Recent discoveries and controversies in plant G-protein signal transduction&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Johnston&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant Physiol%5BTitle%5D%29 AND 131%5BVolume%5D AND 1623%5BPagination%5D AND Jones AM%2C Ecker JR%2C Chen J%2DG%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Jones&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=A Reevaluation of the Role of the Heterotrimeric G Protein in Coupling Light Responses in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A Reevaluation of the Role of the Heterotrimeric G Protein in Coupling Light Responses in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Jones&as_ylo=2003&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28J%2E Mol%2E Biol%5BTitle%5D%29 AND 287%5BVolume%5D AND 797%5BPagination%5D AND Jones DT%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=GenTHREADER: An Efficient and Reliable Protein Fold Recognition Method for Genomic Sequences&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Jones&as_ylo=1999&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28J%2E Mol%2E Biol%5BTitle%5D%29 AND 292%5BVolume%5D AND 195%5BPagination%5D AND Jones DT%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=Protein secondary structure prediction based on position-specific scoring matrices&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Jones&as_ylo=1999&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28The Crystal Structure of a Self%2DActivating G Protein %3F Subunit Reveals Its Distinct Mechanism of Signal Initiation%2E%5BTitle%5D%29 AND Jones JC%2C Duffy JW%2C Machius M%2C Temple BRS%2C Dohlman HG%2C Jones AM%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=The Crystal Structure of a Self-Activating G Protein ? Subunit Reveals Its Distinct Mechanism of Signal Initiation.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The Crystal Structure of a Self-Activating G Protein ? Subunit Reveals Its Distinct Mechanism of Signal Initiation.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Jones&as_ylo=2011&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28J%2E Biol%2E Chem%5BTitle%5D%29 AND 286%5BVolume%5D AND 13143%5BPagination%5D AND Jones JC%2C Temple BRS%2C Jones AM%2C Dohlman HG%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Jones JC, Temple BRS, Jones AM, Dohlman HG (2011b) Functional Reconstitution of an Atypical G Protein Heterotrimer and Regulator of G Protein Signaling Protein (RGS1) from Arabidopsis thaliana. J. Biol. Chem. 286: 13143-13150


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http://scholar.google.com/scholar?as_q=Functional Reconstitution of an Atypical G Protein Heterotrimer and Regulator of G Protein Signaling Protein (RGS1) from Arabidopsis thaliana&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Jones&as_ylo=2011&as_allsubj=all&hl=en&c2coff=1



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Kosugi S, Hasebe M, Tomita M, Yanagawa H (2008) Nuclear Export Signal Consensus Sequences Defined Using a Localization-Based Yeast Selection System. Traffic 9: 2053-2062


la Cour T, Kiemer L, Molgaard A, Gupta R, Skriver K, Brunak S (2004) Analysis and prediction of leucine-rich nuclear exportsignals. Protein Eng. Des. Sel. 17: 527-536


Lease KA, Wen JQ, Li J, Doke JT, Liscum E, Walker JC (2001) A Mutant Arabidopsis Heterotrimeric G-Protein ? Subunit AffectsLeaf, Flower, and Fruit Development. Plant Cell 13: 2631-2641


Lee YRJ, Assmann SM (1999) Arabidopsis thaliana 'extra-large GTP-binding protein' (AtXLG1): a new class of G-protein. PlantMol.Biol. 40: 55-64


Li SJ, Liu YJ, Zheng LY, Chen LL, Li N, Corke F, Lu YR, Fu XD, Zhu ZG, Bevan MW, Li YH (2012) The plant-specific G protein ?subunit AGG3 influences organ size and shape in Arabidopsis thaliana. New Phytol. 194: 690-703


Liu JM, Ding PT, Sun TJ, Nitta Y, Dong O, Huang XC, Yang W, Li X, Botella JR, Zhang YL (2013) Heterotrimeric G Proteins Serve asa Converging Point in Plant Defense Signaling Activated by Multiple Receptor-Like Kinases. Plant Physiol. 161: 2146-2158


Liu JX, Howell SH (2010) Endoplasmic Reticulum Protein Quality Control and Its Relationship to Environmental Stress Responsesin Plants. Plant Cell 22: 2930-2942


Llorente F, Alonso-Blanco C, Sanchez-Rodriguez C, Jorda L, Molina A (2005) ERECTA receptor-like kinase and heterotrimeric G www.plantphysiol.orgon June 13, 2018 - Published by Downloaded from

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Pandey S, Monshausen GB, Ding L, Assmann SM (2008) Regulation of root-wave response by extra large and conventional Gproteins in Arabidopsis thaliana. Plant J. 55: 311-322


Pandey S, Nelson DC, Assmann SM (2009) Two Novel GPCR-Type G Proteins Are Abscisic Acid Receptors in Arabidopsis. Cell 136:136-148


Partow S, Siewers V, Bjorn S, Nielsen J, Maury J (2010) Characterization of different promoters for designing a new expressionvector in Saccharomyces cerevisiae. Yeast 27: 955-964


Plakidou-Dymock S, Dymock D, Hooley R (1998) A higher plant seven-transmembrane receptor that influences sensitivity tocytokinins. Curr. Biol. 8: 315-324


Schroder M, Kaufman RJ (2005) ER stress and the unfolded protein response. Mutat. Res.-Fundam. Mol. Mech. Mutagen. 569: 29-63


Taddese B, Upton GJG, Bailey GR, Jordan SRD, Abdulla NY, Reeves PJ, Reynolds CA (2014) Do Plants Contain G Protein-CoupledReceptors? Plant Physiol. 164: 287-307


Thung L, Chakravorty D, Trusov Y, Jones AM, Botella JR (2013) Signaling Specificity Provided by the Arabidopsis thalianaHeterotrimeric G-Protein ? Subunits AGG1 and AGG2 Is Partially but Not Exclusively Provided through Transcriptional Regulation.PLoS One 8: e58503


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http://scholar.google.com/scholar?as_q=A higher plant seven-transmembrane receptor that influences sensitivity to cytokinins&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Mutat%2E Res%2E%2DFundam%2E Mol%2E Mech%2E Mutagen%5BTitle%5D%29 AND 569%5BVolume%5D AND 29%5BPagination%5D AND Schroder M%2C Kaufman RJ%5BAuthor%5D&dopt=abstract

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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant Physiol%5BTitle%5D%29 AND 164%5BVolume%5D AND 287%5BPagination%5D AND Taddese B%2C Upton GJG%2C Bailey GR%2C Jordan SRD%2C Abdulla NY%2C Reeves PJ%2C Reynolds CA%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=Do Plants Contain G Protein-Coupled Receptors&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Taddese&as_ylo=2014&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Signaling Specificity Provided by the Arabidopsis thaliana Heterotrimeric G%2DProtein %3F Subunits AGG1 and AGG2 Is Partially but Not Exclusively Provided through Transcriptional Regulation%2E%5BTitle%5D%29 AND Thung L%2C Chakravorty D%2C Trusov Y%2C Jones AM%2C Botella JR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Thung L, Chakravorty D, Trusov Y, Jones AM, Botella JR (2013) Signaling Specificity Provided by the Arabidopsis thaliana Heterotrimeric G-Protein ? Subunits AGG1 and AGG2 Is Partially but Not Exclusively Provided through Transcriptional Regulation. PLoS One 8: e58503

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Thung&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Signaling Specificity Provided by the Arabidopsis thaliana Heterotrimeric G-Protein ? Subunits AGG1 and AGG2 Is Partially but Not Exclusively Provided through Transcriptional Regulation.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Signaling Specificity Provided by the Arabidopsis thaliana Heterotrimeric G-Protein ? Subunits AGG1 and AGG2 Is Partially but Not Exclusively Provided through Transcriptional Regulation.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Thung&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%281 %2B G%3F2 %2B G%3F3 %3D G%3F%3A The search for heterotrimeric G%2Dprotein %3F subunits in Arabidopsis is over%2E J%2E Plant Physiol%5BTitle%5D%29 AND 169%5BVolume%5D AND 542%5BPagination%5D AND Thung L%2C Trusov Y%2C Chakravorty D%2C Botella JR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Thung L, Trusov Y, Chakravorty D, Botella JR (2012) G?1 + G?2 + G?3 = G?: The search for heterotrimeric G-protein ? subunits in Arabidopsis is over. J. Plant Physiol. 169: 542-545

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Thung&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=G&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=G&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Thung&as_ylo=2012&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Mol%2E Plant%2DMicrobe Interact%5BTitle%5D%29 AND 26%5BVolume%5D AND 686%5BPagination%5D AND Torres MA%2C Morales J%2C Sanchez%2DRodriguez C%2C Molina A%2C Dangl JL%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Torres MA, Morales J, Sanchez-Rodriguez C, Molina A, Dangl JL (2013) Functional Interplay Between Arabidopsis NADPH Oxidases and Heterotrimeric G Protein. Mol. Plant-Microbe Interact. 26: 686-694

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Torres&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Functional Interplay Between Arabidopsis NADPH Oxidases and Heterotrimeric G Protein&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Functional Interplay Between Arabidopsis NADPH Oxidases and Heterotrimeric G Protein&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Torres&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant Physiol%5BTitle%5D%29 AND 140%5BVolume%5D AND 210%5BPagination%5D AND Trusov Y%2C Rookes JE%2C Chakravorty D%2C Armour D%2C Schenk PM%2C Botella JR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Trusov Y, Rookes JE, Chakravorty D, Armour D, Schenk PM, Botella JR (2006) Heterotrimeric G Proteins Facilitate Arabidopsis Resistance to Necrotrophic Pathogens and Are Involved in Jasmonate Signaling. Plant Physiol. 140: 210-220

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Trusov&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Heterotrimeric G Proteins Facilitate Arabidopsis Resistance to Necrotrophic Pathogens and Are Involved in Jasmonate Signaling&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Heterotrimeric G Proteins Facilitate Arabidopsis Resistance to Necrotrophic Pathogens and Are Involved in Jasmonate Signaling&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Trusov&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Subunits Provide Functional Selectivity in G%3F%3F Dimer Signaling in Arabidopsis%2E Plant Cell%5BTitle%5D%29 AND 19%5BVolume%5D AND 1235%5BPagination%5D AND Trusov Y%2C Rookes JE%2C Tilbrook K%2C Chakravorty D%2C Mason MG%2C Anderson D%2C Chen JG%2C Jones AM%2C Botella JR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Trusov Y, Rookes JE, Tilbrook K, Chakravorty D, Mason MG, Anderson D, Chen JG, Jones AM, Botella JR (2007) Heterotrimeric G Protein ? Subunits Provide Functional Selectivity in G?? Dimer Signaling in Arabidopsis. Plant Cell 19: 1235-1250


http://scholar.google.com/scholar?as_q=Heterotrimeric G Protein&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Heterotrimeric G Protein&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Trusov&as_ylo=2007&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%281 %2B G%3F2 %21%3D G%3F%3A Heterotrimeric G Protein G%3F%2DDeficient Mutants Do Not Recapitulate All Phenotypes of G%3F%2DDeficient Mutants%2E Plant Physiol%5BTitle%5D%29 AND 147%5BVolume%5D AND 636%5BPagination%5D AND Trusov Y%2C Zhang W%2C Assmann SM%2C Botella JR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Trusov Y, Zhang W, Assmann SM, Botella JR (2008) G?1 + G?2 != G?: Heterotrimeric G Protein G?-Deficient Mutants Do Not Recapitulate All Phenotypes of G?-Deficient Mutants. Plant Physiol. 147: 636-649


http://scholar.google.com/scholar?as_q=G&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=G&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Trusov&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Science%5BTitle%5D%29 AND 311%5BVolume%5D AND 239%5BPagination%5D AND Uetz P%2C Dong YA%2C Zeretzke C%2C Atzler C%2C Baiker A%2C Berger B%2C Rajagopala SV%2C Roupelieva M%2C Rose D%2C Fossum E%2C Haas J%5BAuthor%5D&dopt=abstract

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http://scholar.google.com/scholar?as_q=Herpesviral Protein Networks and Their Interaction with the Human Proteome&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Herpesviral Protein Networks and Their Interaction with the Human Proteome&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Uetz&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1


Ullah H, Chen JG, Temple B, Boyes DC, Alonso JM, Davis KR, Ecker JR, Jones AM (2003) The ?-Subunit of the Arabidopsis GProtein Negatively Regulates Auxin-Induced Cell Division and Affects Multiple Developmental Processes. Plant Cell 15: 393-409


Ullah H, Chen JG, Wang SC, Jones AM (2002) Role of a Heterotrimeric G Protein in Regulation of Arabidopsis Seed Germination.Plant Physiol. 129: 897-907


Ullah H, Chen JG, Young JC, Im KH, Sussman MR, Jones AM (2001) Modulation of Cell Proliferation by Heterotrimeric G Protein inArabidopsis. Science 292: 2066-2069


Urano D, Colaneri A, Jones AM (2014) Ga modulates salt-induced cellular senescence and cell division in rice and maize. J. Exp.Bot. 65: 6553-6561


Urano D, Jones JC, Wang H, Matthews M, Bradford W, Bennetzen JL, Jones AM (2012a) G Protein Activation without a GEF in thePlant Kingdom. PLoS Genet. 8: e1002756


Urano D, Phan N, Jones JC, Yang J, Huang JR, Grigston J, Taylor JP, Jones AM (2012b) Endocytosis of the seven-transmembraneRGS1 protein activates G-protein-coupled signalling in Arabidopsis. Nat. Cell Biol. 14: 1079-1088


Ursic D, Chinchilla K, Finkel JS, Culbertson MR (2004) Multiple protein/protein and protein/RNA interactions suggest roles foryeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing. Nucleic Acids Res. 32:2441-2452


Wall MA, Posner BA, Sprang SR (1998) Structural basis of activity and subunit recognition in G protein heterotrimers. Structurewith Folding & Design 6: 1169-1183


Wang HX, Weerasinghe RR, Perdue TD, Cakmakci NG, Taylor JP, Marzluff WF, Jones AM (2006) A Golgi-localized HexoseTransporter Is Involved in Heterotrimeric G Protein-mediated Early Development in Arabidopsis. Mol. Biol. Cell 17: 4257-4269


Wang MY, Xu QY, Yuan M (2011) The Unfolded Protein Response Induced by Salt Stress in Arabidopsis. Methods in Enzymology489: 319-328


Wang SY, Narendra S, Fedoroff N (2007) Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response. Proc.Natl. Acad. Sci. U. S. A. 104: 3817-3822


Wang XQ, Ullah H, Jones AM, Assmann SM (2001) G Protein Regulation of Ion Channels and Abscisic Acid Signaling in ArabidopsisGuard Cells. Science 292: 2070-2072


Warpeha KM, Gibbons J, Carol A, Slusser J, Tree R, Durham W, Kaufman LS (2008) Adequate phenylalanine synthesis mediated byG protein is critical for protection from UV radiation damage in young etiolated Arabidopsis thaliana seedlings. Plant Cell Environ.31: 1756-1770



http://www.ncbi.nlm.nih.gov/pubmed?term=%28Subunit of the Arabidopsis G Protein Negatively Regulates Auxin%2DInduced Cell Division and Affects Multiple Developmental Processes%2E Plant Cell%5BTitle%5D%29 AND 15%5BVolume%5D AND 393%5BPagination%5D AND Ullah H%2C Chen JG%2C Temple B%2C Boyes DC%2C Alonso JM%2C Davis KR%2C Ecker JR%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Ullah H, Chen JG, Temple B, Boyes DC, Alonso JM, Davis KR, Ecker JR, Jones AM (2003) The ?-Subunit of the Arabidopsis G Protein Negatively Regulates Auxin-Induced Cell Division and Affects Multiple Developmental Processes. Plant Cell 15: 393-409

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Ullah&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ullah&as_ylo=2003&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant Physiol%5BTitle%5D%29 AND 129%5BVolume%5D AND 897%5BPagination%5D AND Ullah H%2C Chen JG%2C Wang SC%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Ullah H, Chen JG, Wang SC, Jones AM (2002) Role of a Heterotrimeric G Protein in Regulation of Arabidopsis Seed Germination. Plant Physiol. 129: 897-907


http://scholar.google.com/scholar?as_q=Role of a Heterotrimeric G Protein in Regulation of Arabidopsis Seed Germination&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Role of a Heterotrimeric G Protein in Regulation of Arabidopsis Seed Germination&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ullah&as_ylo=2002&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Science%5BTitle%5D%29 AND 292%5BVolume%5D AND 2066%5BPagination%5D AND Ullah H%2C Chen JG%2C Young JC%2C Im KH%2C Sussman MR%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Ullah H, Chen JG, Young JC, Im KH, Sussman MR, Jones AM (2001) Modulation of Cell Proliferation by Heterotrimeric G Protein in Arabidopsis. Science 292: 2066-2069


http://scholar.google.com/scholar?as_q=Modulation of Cell Proliferation by Heterotrimeric G Protein in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Modulation of Cell Proliferation by Heterotrimeric G Protein in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ullah&as_ylo=2001&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28J%2E Exp%2E Bot%5BTitle%5D%29 AND 65%5BVolume%5D AND 6553%5BPagination%5D AND Urano D%2C Colaneri A%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Urano D, Colaneri A, Jones AM (2014) Ga modulates salt-induced cellular senescence and cell division in rice and maize. J. Exp. Bot. 65: 6553-6561

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Urano&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Ga modulates salt-induced cellular senescence and cell division in rice and maize&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Ga modulates salt-induced cellular senescence and cell division in rice and maize&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Urano&as_ylo=2014&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28G Protein Activation without a GEF in the Plant Kingdom%2E%5BTitle%5D%29 AND Urano D%2C Jones JC%2C Wang H%2C Matthews M%2C Bradford W%2C Bennetzen JL%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Urano D, Jones JC, Wang H, Matthews M, Bradford W, Bennetzen JL, Jones AM (2012a) G Protein Activation without a GEF in the Plant Kingdom. PLoS Genet. 8: e1002756


http://scholar.google.com/scholar?as_q=G Protein Activation without a GEF in the Plant Kingdom.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=G Protein Activation without a GEF in the Plant Kingdom.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Urano&as_ylo=2012&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Nat%2E Cell Biol%5BTitle%5D%29 AND 14%5BVolume%5D AND 1079%5BPagination%5D AND Urano D%2C Phan N%2C Jones JC%2C Yang J%2C Huang JR%2C Grigston J%2C Taylor JP%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Urano D, Phan N, Jones JC, Yang J, Huang JR, Grigston J, Taylor JP, Jones AM (2012b) Endocytosis of the seven-transmembrane RGS1 protein activates G-protein-coupled signalling in Arabidopsis. Nat. Cell Biol. 14: 1079-1088


http://scholar.google.com/scholar?as_q=Endocytosis of the seven-transmembrane RGS1 protein activates G-protein-coupled signalling in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Endocytosis of the seven-transmembrane RGS1 protein activates G-protein-coupled signalling in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Urano&as_ylo=2012&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Nucleic Acids Res%5BTitle%5D%29 AND 32%5BVolume%5D AND 2441%5BPagination%5D AND Ursic D%2C Chinchilla K%2C Finkel JS%2C Culbertson MR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Ursic D, Chinchilla K, Finkel JS, Culbertson MR (2004) Multiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing. Nucleic Acids Res. 32: 2441-2452

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Ursic&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Multiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Multiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ursic&as_ylo=2004&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Structure with Folding %26 Design%5BTitle%5D%29 AND 6%5BVolume%5D AND 1169%5BPagination%5D AND Wall MA%2C Posner BA%2C Sprang SR%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wall MA, Posner BA, Sprang SR (1998) Structural basis of activity and subunit recognition in G protein heterotrimers. Structure with Folding & Design 6: 1169-1183

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Wall&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Structural basis of activity and subunit recognition in G protein heterotrimers&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Structural basis of activity and subunit recognition in G protein heterotrimers&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wall&as_ylo=1998&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Mol%2E Biol%2E Cell%5BTitle%5D%29 AND 17%5BVolume%5D AND 4257%5BPagination%5D AND Wang HX%2C Weerasinghe RR%2C Perdue TD%2C Cakmakci NG%2C Taylor JP%2C Marzluff WF%2C Jones AM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wang HX, Weerasinghe RR, Perdue TD, Cakmakci NG, Taylor JP, Marzluff WF, Jones AM (2006) A Golgi-localized Hexose Transporter Is Involved in Heterotrimeric G Protein-mediated Early Development in Arabidopsis. Mol. Biol. Cell 17: 4257-4269

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Wang&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=A Golgi-localized Hexose Transporter Is Involved in Heterotrimeric G Protein-mediated Early Development in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A Golgi-localized Hexose Transporter Is Involved in Heterotrimeric G Protein-mediated Early Development in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wang&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Methods in Enzymology%5BTitle%5D%29 AND 489%5BVolume%5D AND 319%5BPagination%5D AND Wang MY%2C Xu QY%2C Yuan M%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wang MY, Xu QY, Yuan M (2011) The Unfolded Protein Response Induced by Salt Stress in Arabidopsis. Methods in Enzymology 489: 319-328


http://scholar.google.com/scholar?as_q=The Unfolded Protein Response Induced by Salt Stress in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The Unfolded Protein Response Induced by Salt Stress in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wang&as_ylo=2011&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Proc%2E Natl%2E Acad%2E Sci%2E U%2E S%2E A%5BTitle%5D%29 AND 104%5BVolume%5D AND 3817%5BPagination%5D AND Wang SY%2C Narendra S%2C Fedoroff N%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wang SY, Narendra S, Fedoroff N (2007) Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response. Proc. Natl. Acad. Sci. U. S. A. 104: 3817-3822


http://scholar.google.com/scholar?as_q=Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wang&as_ylo=2007&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=%28Science%5BTitle%5D%29 AND 292%5BVolume%5D AND 2070%5BPagination%5D AND Wang XQ%2C Ullah H%2C Jones AM%2C Assmann SM%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wang XQ, Ullah H, Jones AM, Assmann SM (2001) G Protein Regulation of Ion Channels and Abscisic Acid Signaling in Arabidopsis Guard Cells. Science 292: 2070-2072


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http://www.ncbi.nlm.nih.gov/pubmed?term=%28Plant Cell Environ%5BTitle%5D%29 AND 31%5BVolume%5D AND 1756%5BPagination%5D AND Warpeha KM%2C Gibbons J%2C Carol A%2C Slusser J%2C Tree R%2C Durham W%2C Kaufman LS%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Warpeha KM, Gibbons J, Carol A, Slusser J, Tree R, Durham W, Kaufman LS (2008) Adequate phenylalanine synthesis mediated by G protein is critical for protection from UV radiation damage in young etiolated Arabidopsis thaliana seedlings. Plant Cell Environ. 31: 1756-1770

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Warpeha KM, Lateef SS, Lapik Y, Anderson M, Lee BS, Kaufman LS (2006) G-Protein-Coupled Receptor 1, G-Protein G?-Subunit 1,and Prephenate Dehydratase 1 Are Required for Blue Light-Induced Production of Phenylalanine in Etiolated Arabidopsis. PlantPhysiol. 140: 844-855


Warpeha KM, Upadhyay S, Yeh J, Adamiak J, Hawkins SI, Lapik YR, Anderson MB, Kaufman LS (2007) The GCR1, GPA1, PRN1, NF-Y Signal Chain Mediates Both Blue Light and Abscisic Acid Responses in Arabidopsis. Plant Physiol. 143: 1590-1600


Wei Q, Zhou WB, Hu GZ, Wei JM, Yang HQ, Huang JR (2008) Heterotrimeric G-protein is involved in phytochrome A-mediated celldeath of Arabidopsis hypocotyls. Cell Research 18: 949-960


Weiss C, Garnaat C, Mukai K, Hu Y, Ma H (1994) Isolation of cDNAs encoding guanine nucleotide-binding protein ?-subunithomologues from maize (ZGB1) and Arabidopsis (AGB1). Proc. Natl. Acad. Sci. U. S. A. 91: 9554-9558


Wiederstein M, Sippl MJ (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structuresof proteins. Nucleic Acids Res. 35: W407-W410


Wolfenstetter S, Chakravorty D, Kula R, Urano D, Trusov Y, Sheahan MB, McCurdy DW, Assmann SM, Jones AM, Botella JR (2015)Evidence for an unusual transmembrane configuration of AGG3, a class C G? subunit of Arabidopsis. The Plant Journal 81: 388-398


Xu DR, Grishin NV, Chook YM (2012) NESdb: a database of NES-containing CRM1 cargoes. Mol. Biol. Cell 23: 3673-3676Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Yachdav G, Kloppmann E, Kajan L, Hecht M, Goldberg T, Hamp T, Honigschmid P, Schafferhans A, Roos M, Bernhofer M, RichterL, Ashkenazy H, Punta M, Schlessinger A, Bromberg Y, Schneider R, Vriend G, Sander C, Ben-Tal N, Rost B (2014) PredictProtein-an open resource for online prediction of protein structural and functional features. Nucleic Acids Res. 42: W337-W343


Yu Y, Assmann SM (2015) The heterotrimeric G-protein ß subunit, AGB1, plays multiple roles in the Arabidopsis salinity response.Plant, Cell & Environment: PMID: 25808946


Zhang LG, Hu GZ, Cheng YX, Huang JR (2008) Heterotrimeric G protein ? and ? subunits antagonistically modulate stomataldensity in Arabidopsis thaliana. Dev. Biol. 324: 68-75


Zhao J, Wang XM (2004) Arabidopsis Phospholipase D?1 Interacts with the Heterotrimeric G-protein ?-Subunit through a MotifAnalogous to the DRY Motif in G-protein-coupled Receptors. J. Biol. Chem. 279: 1794-1800


Zhu HF, Li GJ, Ding L, Cui XQ, Berg H, Assmann SM, Xia YJ (2009) Arabidopsis Extra Large G-Protein 2 (XLG2) Interacts with theG? Subunit of Heterotrimeric G Protein and Functions in Disease Resistance. Mol. Plant. 2: 513-525



http://www.ncbi.nlm.nih.gov/pubmed?term=%28G%5BTitle%5D%29 AND 1%5BVolume%5D AND Warpeha KM%2C Lateef SS%2C Lapik Y%2C Anderson M%2C Lee BS%2C Kaufman LS%5BAuthor%5D&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Warpeha KM, Lateef SS, Lapik Y, Anderson M, Lee BS, Kaufman LS (2006) G-Protein-Coupled Receptor 1, G-Protein G?-Subunit 1, and Prephenate Dehydratase 1 Are Required for Blue Light-Induced Production of Phenylalanine in Etiolated Arabidopsis. Plant Physiol. 140: 844-855



http://scholar.google.com/scholar?as_q=&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Warpeha&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

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http://search.crossref.org/?page=1&rows=2&q=Warpeha KM, Upadhyay S, Yeh J, Adamiak J, Hawkins SI, Lapik YR, Anderson MB, Kaufman LS (2007) The GCR1, GPA1, PRN1, NF-Y Signal Chain Mediates Both Blue Light and Abscisic Acid Responses in Arabidopsis. Plant Physiol. 143: 1590-1600



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http://search.crossref.org/?page=1&rows=2&q=Wei Q, Zhou WB, Hu GZ, Wei JM, Yang HQ, Huang JR (2008) Heterotrimeric G-protein is involved in phytochrome A-mediated cell death of Arabidopsis hypocotyls. Cell Research 18: 949-960

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http://www.ncbi.nlm.nih.gov/pubmed?term=%28subunit homologues from maize ZGB1 and Arabidopsis AGB1%2E Proc%2E Natl%2E Acad%2E Sci%2E U%2E S%2E A%5BTitle%5D%29 AND 91%5BVolume%5D AND 9554%5BPagination%5D AND Weiss C%2C Garnaat C%2C Mukai K%2C Hu Y%2C Ma H%5BAuthor%5D&dopt=abstract

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Running Head: XLGs in heterotrimeric G protein signaling ... · 6 and siliques (Lease et al., 2001), as well as in pathogen responses (Llorente et al., 2005; Trusov et al., 2006;