Publication Information
Benschop et al., 2007
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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]