MCP
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/mcp.M600429-MCP200 on February 21, 2007.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M600429-MCP200v1
6/7/1198    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Benschop, J. J.
Right arrow Articles by Menke, F. L. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Benschop, J. J.
Right arrow Articles by Menke, F. L. H.
Molecular & Cellular Proteomics 6:1198-1214, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Quantitative Phosphoproteomics of Early Elicitor Signaling in Arabidopsis*,S

Joris J. Benschop{ddagger},§,¶, Shabaz Mohammed§,||, Martina O'Flaherty||, Albert J. R. Heck||, Monique Slijper||,** and Frank L. H. Menke{ddagger},{ddagger}{ddagger}

From the {ddagger} Molecular Genetics, Utrecht University, Padualaan 8, 3584CH Utrecht, The Netherlands and || Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584CA 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.

** To whom correspondence may be addressed. E-mail: m.slijper{at}pharm.uu.nl

{ddagger}{ddagger} To whom correspondence may be addressed. E-mail: f.l.h.menke{at}bio.uu.nl




This article has been cited by other articles:


Home page
 Mol PlantHome page
Z. Zhang, A. Lenk, M. X. Andersson, T. Gjetting, C. Pedersen, M. E. Nielsen, M.-A. Newman, B.-H. Hou, S. C. Somerville, and H. Thordal-Christensen
A Lesion-Mimic Syntaxin Double Mutant in Arabidopsis Reveals Novel Complexity of Pathogen Defense Signaling
Mol Plant, April 15, 2008; (2008) ssn011v1.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
W. Tang, Z. Deng, J. A. Oses-Prieto, N. Suzuki, S. Zhu, X. Zhang, A. L. Burlingame, and Z.-Y. Wang
Proteomics Studies of Brassinosteroid Signal Transduction Using Prefractionation and Two-dimensional DIGE
Mol. Cell. Proteomics, April 1, 2008; 7(4): 728 - 738.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
R. Hebeler, S. Oeljeklaus, K. A. Reidegeld, M. Eisenacher, C. Stephan, B. Sitek, K. Stuhler, H. E. Meyer, M. J. G. Sturre, P. P. Dijkwel, et al.
Study of Early Leaf Senescence in Arabidopsis thaliana by Quantitative Proteomics Using Reciprocal 14N/15N Labeling and Difference Gel Electrophoresis
Mol. Cell. Proteomics, January 1, 2008; 7(1): 108 - 120.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
J. J. Thelen and S. C. Peck
Quantitative Proteomics in Plants: Choices in Abundance
PLANT CELL, November 1, 2007; 19(11): 3339 - 3346.
[Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
T. Niittyla, A. T. Fuglsang, M. G. Palmgren, W. B. Frommer, and W. X. Schulze
Temporal Analysis of Sucrose-induced Phosphorylation Changes in Plasma Membrane Proteins of Arabidopsis
Mol. Cell. Proteomics, October 1, 2007; 6(10): 1711 - 1726.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.