The Microbe Associated Molecular Pattern flg22 is recognized in a FLAGELLIN-SENSITVE 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 wildtype 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 ATBa, a substrate subunit of a protein phosphatase 2A complex and an interactor to 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 ATBa strongly increases basal endocytosis of AtRGS1. AtRGS1 steady-state protein level is lower in the atba 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 regulation of system dynamics in innate immunity. The PP2A(ATBa) complex is a critical regulator of this signaling pathway
[doi:10.25345/C5MP4VZ4B]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: flg22 ; phosphoproteomics of flg22 induced arabidopsis ; 22-amino peptide released from bacterial flagellin ; AtRGS1
Principal Investigators: (in alphabetical order) |
Alan Jones, UNC Chapel Hill, United States Justin Walley, Iowa State University, US |
Submitting User: | chrisfm |
Watkins JM, Montes C, Clark NM, Song G, Oliveira CC, Mishra B, Brachova L, Seifert CM, Mitchell MS, Yang J, Braga Dos Reis PA, Urano D, Muktar MS, Walley JW, Jones AM.
Phosphorylation Dynamics in a flg22-Induced, G Protein-Dependent Network Reveals the AtRGS1 Phosphatase.
Mol Cell Proteomics. 2024 Feb;23(2):100705. Epub 2023 Dec 20.
Number of Files: | |
Total Size: | |
Spectra: | |
Subscribers: | |
Owner | Reanalyses | |
---|---|---|
Experimental Design | ||
Conditions:
|
||
Biological Replicates:
|
||
Technical Replicates:
|
||
Identification Results | ||
Proteins (Human, Remapped):
|
||
Proteins (Reported):
|
||
Peptides:
|
||
Variant Peptides:
|
||
PSMs:
|
||
Quantification Results | ||
Differential Proteins:
|
||
Quantified Proteins:
|
||
Browse Dataset Files | Browse Results |
FTP Download Link (click to copy):
|