Saltational evolution of the heterotrimeric G protein signaling mechanisms in the plant kingdom

Urano, Daisuke; Maruta, Natsumi; Trusov, Yuri; Stoian, Richard; Wu, Qingyu; Liang, Ying; Jaiswal, Dinesh Kumar; Thung, Leena; Jackson, David; Botella, José Ramón; Jones, Alan M.

doi:10.1126/scisignal.aaf9558

Cited by 74 publications

(88 citation statements)

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“…The human genome encodes 23 Gα, 5 Gβ, and 12 Gγ subunits, ~850 GPCRs, and ~40 RGS proteins. In Arabidopsis, the heterotrimeric G protein complex consist of one canonical alpha subunit (AtGPA1), one beta subunit ( AGB1 ), one of three gamma subunits (AGG1, 2, and 3), at least one subunit of Regulator of G Signaling protein (AtRGS1), and one of three atypical Extra-Large G proteins (XLG1, 2, and 3) (Pandey et al, 2006; Ding et al, 2008; Chakravorty et al, 2011; Urano et al, 2013, 2016; Wolfenstetter et al, 2015) in lieu of the canonical G subunit. In plants, the mechanism for activation is different than in animals; the Gα subunit self-activates without a GPCR and instead is kept in the basal state by a 7 transmembrane RGS protein (Urano et al, 2012, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…The primary sequence conservation of the C-terminal Gα domain of the three XLG proteins compared to the canonical Gα are 26.1, 23.2, and 28.5% identities for XLG1 446–888 , XLG2 435–861 , and XLG3 396–848 , respectively (Ding et al, 2008; Chakravorty et al, 2015; Urano et al, 2016). The Gα domain of XLGs is structurally similar to AtGPA1 containing three of five G-box motifs that are critical for binding the guanine nucleotide.…”

Section: Introductionmentioning

confidence: 99%

“…Whether or not XLGs bind guanine nucleotides is unclear but the evidence to date indicate that if they do, the mode is different from the canonical Gα subunit (Lee and Assmann, 1999; Heo et al, 2012). In vitro studies indicate that XLGs bind the Gβγ dimer but do so unlike the canonical Gα subunit (Maruta et al, 2015) and possibly do so independently of nucleotide binding (Urano et al, 2016). Finally, there is uncertainty in the literature about the subcellular location of XLGs.…”

Section: Introductionmentioning

confidence: 99%

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Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization

2017

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The three-member family of Arabidopsis extra-large G proteins (XLG1-3) defines the prototype of an atypical Gα subunit in the heterotrimeric G protein complex. Recent evidence indicate that XLG subunits operate along with its Gβγ dimer in root morphology, stress responsiveness, and cytokinin induced development, however downstream targets of activated XLG proteins in the stress pathways are rarely known. To assemble a set of candidate XLG-targeted proteins, a yeast two-hybrid complementation-based screen was performed using XLG protein baits to query interactions between XLG and partner protein found in glucose-treated seedlings, roots, and Arabidopsis cells in culture. Seventy two interactors were identified and >60% of a test set displayed in vivo interaction with XLG proteins. Gene co-expression analysis shows that >70% of the interactors are positively correlated with the corresponding XLG partners. Gene Ontology enrichment for all the candidates indicates stress responses and posits a molecular mechanism involving a specific set of transcription factor partners to XLG. Genes encoding two of these transcription factors, SZF1 and 2, require XLG proteins for full NaCl-induced expression. The subcellular localization of the XLG proteins in the nucleus, endosome, and plasma membrane is dependent on the specific interacting partner.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization

2017

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“…In this study, we used the following T-DNA insertion mutant alleles: agb1 - 2 [19], rgs1 - 2 [20], gpa1 - 3 [21], xlg1xlg2xlg3 [13] which combines these alleles xlg1 - 1 (SAIL_760H08) [13], xlg2 - 2 (SALK_062645), xlg3 - 2 (SAIL_107656) [13], and xlg/gpa1 which combines the xlg1 - 1 , xlg2 - 1 , xlg3 - 2 and gpa1 - 3 alleles above [22] (in press).A digital camera that captures images in RAW format.X-rite ColorChecker classic chart (http://xritephoto.com/colorchecker-classic). …”

Section: Materials Neededmentioning

confidence: 99%

A nondestructive method to estimate the chlorophyll content of Arabidopsis seedlings

et al. 2017

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BackgroundChlorophyll content decreases in plants under stress conditions, therefore it is used commonly as an indicator of plant health. Arabidopsis thaliana offers a convenient and fast way to test physiological phenotypes of mutations and treatments. However, chlorophyll measurements with conventional solvent extraction are not applicable to Arabidopsis leaves due to their small size, especially when grown on culture dishes.ResultsWe provide a nondestructive method for chlorophyll measurement whereby the red, green and blue (RGB) values of a color leaf image is used to estimate the chlorophyll content from Arabidopsis leaves. The method accommodates different profiles of digital cameras by incorporating the ColorChecker chart to make the digital negative profiles, to adjust the white balance, and to calibrate the exposure rate differences caused by the environment so that this method is applicable in any environment. We chose an exponential function model to estimate chlorophyll content from the RGB values, and fitted the model parameters with physical measurements of chlorophyll contents. As proof of utility, this method was used to estimate chlorophyll content of G protein mutants grown on different sugar to nitrogen ratios.ConclusionThis method is a simple, fast, inexpensive, and nondestructive estimation of chlorophyll content of Arabidopsis seedlings. This method lead to the discovery that G proteins are important in sensing the C/N balance to control chlorophyll content in Arabidopsis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13007-017-0174-6) contains supplementary material, which is available to authorized users.

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“…Loss of function alleles for BRL3 and AtRGS1 do not have gross developmental phenotypes [4,16] and therefore due to a lack of pleotrophy, they are useful for studies on signaling. BRL3 binds brasinolide but has otherwise not yet been implicated in a signaling pathway other than for brassinosteroid.…”

Section: Introductionmentioning

confidence: 99%

BRL3 and AtRGS1 cooperate to fine tune growth inhibition and ROS activation

Tunc‐Ozdemir

Jones

2017

PLoS ONE

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Plasma membrane-localized leucine-rich repeat receptor-like kinases directly activates G protein complex via interaction with seven transmembrane domain Regulator of G-protein Signaling 1 (AtRGS1) protein. Brassinosteroid insensitive 1 (BRI1) LIKE3 (BRL3) phosphorylates AtRGS1 in vitro. FRET analysis showed that BRL3 and AtRGS1 interaction dynamics change in response to glucose and flg22. Both BRL3 and AtRGS1 function in glucose sensing and brl3 and rgs1-2 single mutants are hyposensitive to high glucose as well as the brl3/rgs1 double mutant. BRL3 and AtRGS1 function in the same pathway linked to high glucose sensing. Hypocotyl elongation, another sugar-mediated pathway, is also implicated to be partially mediated by BRL3 and AtRGS1 because rgs1-2, brl3-2 and brl3-2/ rgs1-2 mutants share the long hypocotyl phenotype. BRL3 and AtRGS1 modulate the flg22-induced ROS burst and block one or more components positively regulating ROS production because the brl3/rgs1 double mutant has ~60% more ROS production than wild type while rgs1-2 has a partial ROS burst impairment and brl3 has slightly more ROS production. Here, we proposed a simple model where both BRL3 and AtRGS1 are part of a fine-tuning mechanism sensing glucose and flg22 to prevent excess ROS burst and control growth inhibition.

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Saltational evolution of the heterotrimeric G protein signaling mechanisms in the plant kingdom

Abstract: Rapid diversification of the XLG family of Gα proteins may have enabled plants to adapt to the variable land environment.

Cited by 74 publications

References 44 publications

Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization

Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization

A nondestructive method to estimate the chlorophyll content of Arabidopsis seedlings

BRL3 and AtRGS1 cooperate to fine tune growth inhibition and ROS activation

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