2016 journal article

Direct Modulation of Heterotrimeric G Protein-coupled Signaling by a Receptor Kinase Complex

JOURNAL OF BIOLOGICAL CHEMISTRY, 291(27), 13918–13925.

By: M. Tunc-Ozdemir*, D. Urano *, D. Jaiswal *, S. Clouse n & A. Jones *

author keywords: Arabidopsis thaliana; G protein; phosphorylation; receptor protein serine; threonine kinase; regulator of G protein signaling (RGS); receptor-like kinases; BAK1; FLS2; flg22; AtRGS1
MeSH headings : Arabidopsis / genetics; Arabidopsis / metabolism; Arabidopsis Proteins / genetics; Arabidopsis Proteins / metabolism; Flagellin / pharmacology; Peptides / pharmacology; Phosphorylation / drug effects; Phosphorylation / physiology; Protein Serine-Threonine Kinases / genetics; Protein Serine-Threonine Kinases / metabolism; RGS Proteins / genetics; RGS Proteins / metabolism; Signal Transduction / drug effects; Signal Transduction / physiology
TL;DR: It is proposed that in complete contrast to G protein activation in animals, plant leucine-rich repeat receptor-like kinases (LRR RLKs), not GPCRs, provide this discrimination through phosphorylation of AtRGS1 in a ligand-dependent manner. (via Semantic Scholar)
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Plants and some protists have heterotrimeric G protein complexes that activate spontaneously without canonical G protein-coupled receptors (GPCRs). In Arabidopsis, the sole 7-transmembrane regulator of G protein signaling 1 (AtRGS1) modulates the G protein complex by keeping it in the resting state (GDP-bound). However, it remains unknown how a myriad of biological responses is achieved with a single G protein modulator. We propose that in complete contrast to G protein activation in animals, plant leucine-rich repeat receptor-like kinases (LRR RLKs), not GPCRs, provide this discrimination through phosphorylation of AtRGS1 in a ligand-dependent manner. G protein signaling is directly activated by the pathogen-associated molecular pattern flagellin peptide 22 through its LRR RLK, FLS2, and co-receptor BAK1.