title: Direct Modulation of Heterotrimeric G Protein-coupled Signaling by a Receptor Kinase Complex.
abstract: 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.
authors.affiliation: Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599.
authors.forename: Meral
authors.initials: M
authors.lastname: Tunc-Ozdemir
authors.affiliation: Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Urano
authors.affiliation: Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599.
authors.forename: Dinesh Kumar
authors.initials: DK
authors.lastname: Jaiswal
authors.affiliation: Department of Horticultural Science, North Carolina State University, Raleigh, North Carolina 27695-7609.
authors.forename: Steven D
authors.initials: SD
authors.lastname: Clouse
authors.affiliation: Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599; Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599. Electronic address: alan_jones@unc.edu.
authors.forename: Alan M
authors.initials: AM
authors.lastname: Jones
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D005408:Flagellin / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology; D010766:Phosphorylation / Q000187:drug effects / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D020710:RGS Proteins / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology*
chemical_list: D029681:Arabidopsis Proteins; D010455:Peptides; D020710:RGS Proteins; C477755:RGS1 protein, Arabidopsis; D005408:Flagellin; C463660:BAK1 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases
keywords: Arabidopsis thaliana; AtRGS1; BAK1; FLS2; G protein; flg22; phosphorylation; receptor protein serine/threonine kinase; receptor-like kinases; regulator of G protein signaling (RGS)