Phosphorylation Dynamics in a flg22-Induced, G Protein-Dependent Network Reveals the AtRGS1 Phosphatase.

Autor:	Watkins JM; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA., Montes C; Department of Plant Pathology and Microbiology, Iowa State University, Ames, Iowa, USA., Clark NM; Department of Plant Pathology and Microbiology, Iowa State University, Ames, Iowa, USA., Song G; Department of Plant Pathology and Microbiology, Iowa State University, Ames, Iowa, USA., Oliveira CC; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA; Department of Biochemistry and Molecular Biology/BIOAGRO, Universidade Federal de Viçosa, Viçosa, Brazil., Mishra B; Department of Biology, University of Alabama-Birmingham, Birmingham, Alabama, USA., Brachova L; Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa, USA., Seifert CM; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA., Mitchell MS; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA., Yang J; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA., Braga Dos Reis PA; Department of Biochemistry and Molecular Biology/BIOAGRO, Universidade Federal de Viçosa, Viçosa, Brazil., Urano D; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA., Muktar MS; Department of Biology, University of Alabama-Birmingham, Birmingham, Alabama, USA., Walley JW; Department of Plant Pathology and Microbiology, Iowa State University, Ames, Iowa, USA. Electronic address: jwalley@iastate.edu., Jones AM; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA; Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA. Electronic address: alan_jones@unc.edu.
Jazyk:	angličtina
Zdroj:	Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2024 Feb; Vol. 23 (2), pp. 100705. Date of Electronic Publication: 2023 Dec 20.
DOI:	10.1016/j.mcpro.2023.100705
Abstrakt:	The microbe-associated molecular pattern flg22 is recognized in a flagellin-sensitive 2-dependent manner in root tip cells. Here, we show a rapid and massive change in protein abundance and phosphorylation state of the Arabidopsis root cell proteome in WT and a mutant deficient in heterotrimeric G-protein-coupled signaling. flg22-induced changes fall on proteins comprising a subset of this proteome, the heterotrimeric G protein interactome, and on highly-populated hubs of the immunity network. Approximately 95% of the phosphorylation changes in the heterotrimeric G-protein interactome depend, at least partially, on a functional G protein complex. One member of this interactome is ATBα, a substrate-recognition subunit of a protein phosphatase 2A complex and an interactor to Arabidopsis thaliana Regulator of G Signaling 1 protein (AtRGS1), a flg22-phosphorylated, 7-transmembrane spanning modulator of the nucleotide-binding state of the core G-protein complex. A null mutation of ATBα strongly increases basal endocytosis of AtRGS1. AtRGS1 steady-state protein level is lower in the atbα mutant in a proteasome-dependent manner. We propose that phosphorylation-dependent endocytosis of AtRGS1 is part of the mechanism to degrade AtRGS1, thus sustaining activation of the heterotrimeric G protein complex required for the regulation of system dynamics in innate immunity. The PP2A(ATBα) complex is a critical regulator of this signaling pathway. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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