Phosphorylation dynamics in a flg22-induced, G-protein dependent network reveals the RGS1 phosphatase
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive Plus
ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)
SUBMITTER: 
Justin Walley Alan Jones
PROVIDER: MSV000092672 | MassIVE | Wed Aug 16 09:26:00 BST 2023
REPOSITORIES: MassIVE
Publications
Phosphorylation Dynamics in a flg22-Induced, G Protein-Dependent Network Reveals the AtRGS1 Phosphatase.
Watkins Justin M JM Montes Christian C Clark Natalie M NM Song Gaoyuan G Oliveira Celio Cabral CC Mishra Bharat B Brachova Libuse L Seifert Clara M CM Mitchell Malek S MS Yang Jing J Braga Dos Reis Pedro Augusto PA Urano Daisuke D Muktar M Shahid MS Walley Justin W JW Jones Alan M AM
Molecular & cellular proteomics : MCP 20231220 2
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. A ...[more]
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