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Submitted on November 13, 2006
Revised on February 9, 2007
Accepted on February 21, 2007

Quantitative phospho-proteomics of early elicitor signalling in Arabidopsis

Joris J. Benschop, Shabaz Mohammed, Martina O'Flaherty, Albert J.R. Heck, Monique Slijper, and Frank L.H. Menke

Biology, Utrecht University, Utrecht 3584 CH

Corresponding Author: f.l.h.menke{at}bio.uu.nl

Perception of general elicitors by plant cells initiate signal transduction cascades that are regulated by protein phosphorylation. The earliest signalling events occur within minutes and include ion fluxes across the plasma membrane, activation of mitogen activated protein kinases (MAPK) and the formation of reactive oxygen species. The phosphorylation events that regulate these signalling cascades are largely unknown. Here we present a mass spectrometry based quantitative phospho-proteomics approach which identified differentially phosphorylated sites in signalling and response proteins from Arabidopsis cells treated with either flg22 or xylanase. Our approach was sensitive enough to quantitate phosphorylation on low abundance signalling proteins such as calcium dependent protein kinases (CDPKs) 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 indicates a high degree of complexity at the level of post-translational modification, as exemplified by the complex modification patterns of NADPH oxidase protein RBOHD. Furthermore, the data also suggest that protein translocation and vesicle traffic are important aspects of early signalling and defense in response to general elicitors. Our study presents the largest quantitative Arabidopsis phospho-proteomics 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.


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