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Phosphorylation Early Elicitor Signaling

Phosphorylation in Arabidopsis thaliana

674 modifications in 616 peptides, found in 915 proteins

Experiment Details

Exp 23


Experimental Setup
TissueCell culture
Condition10 min 100 μg/mlxylanase or 1 µM flg22
PTM Enrichment TiO2
MS InstrumentLTQ
MS/MS Search Parameters
Protein DatabaseTAIR
FDR ThresholdMASCOT Score > 50
Search Algorithm(s)MASCOT version 2.1
Precursor Mass Tolerance20 ppm
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsOxidation (M)
Phosphorylation (STY)
Other Information
Comments Phosphat 4.0 - Defined sites (pS/T/Y)


Publication Information

Benschop et al., 2007

PubMed ID: 17317660

No external accession available

Abstract

Mol Cell Proteomics. 2007 Jul;6(7):1198-214. doi: 10.1074/mcp.M600429-MCP200. 
Epub 2007 Feb 21.

Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis.

Benschop JJ(1), Mohammed S, O'Flaherty M, Heck AJ, Slijper M, Menke FL.

Author information:
(1)Molecular Genetics, Utrecht University, Padualaan 8, 3584CH Utrecht, The 
Netherlands.

Perception of general elicitors by plant cells initiates signal transduction 
cascades that are regulated by protein phosphorylation. The earliest signaling 
events occur within minutes and include ion fluxes across the plasma membrane, 
activation of MAPKs, and the formation of reactive oxygen species. The 
phosphorylation events that regulate these signaling cascades are largely 
unknown. Here we present a mass spectrometry-based quantitative 
phosphoproteomics approach that identified differentially phosphorylated sites 
in signaling and response proteins from Arabidopsis cells treated with either 
flg22 or xylanase. Our approach was sensitive enough to quantitate 
phosphorylation on low abundance signaling proteins such as calcium-dependent 
protein kinases and receptor-like kinase family members. With this approach we 
identified one or more differentially phosphorylated sites in 76 
membrane-associated proteins including a number of defense-related proteins. Our 
data on phosphorylation indicate a high degree of complexity at the level of 
post-translational modification as exemplified by the complex modification 
patterns of respiratory burst oxidase protein D. Furthermore the data also 
suggest that protein translocation and vesicle traffic are important aspects of 
early signaling and defense in response to general elicitors. Our study presents 
the largest quantitative Arabidopsis phosphoproteomics data set to date and 
provides a new resource that can be used to gain novel insight into plant 
defense signal transduction and early defense response.

DOI: 10.1074/mcp.M600429-MCP200
PMID: 17317660 [Indexed for MEDLINE]