HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M600429-MCP200v1 6/7/1198    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Benschop, J. J. Articles by Menke, F. L. H. Search for Related Content PubMed PubMed Citation Articles by Benschop, J. J. Articles by Menke, F. L. H. Social Bookmarking                      What's this?

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^,,¶, Shabaz Mohammed^,||, Martina O'Flaherty^||, Albert J. R. Heck^||, Monique Slijper^||,** and Frank L. H. Menke^,

From the 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: f.l.h.menke{at}bio.uu.nl

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. K. Tanz, S. G. Tetu, N. G.F. Vella, and M. Ludwig Loss of the Transit Peptide and an Increase in Gene Expression of an Ancestral Chloroplastic Carbonic Anhydrase Were Instrumental in the Evolution of the Cytosolic C4 Carbonic Anhydrase in Flaveria Plant Physiology, July 1, 2009; 150(3): 1515 - 1529. [Abstract] [Full Text] [PDF]

				S. Reiland, G. Messerli, K. Baerenfaller, B. Gerrits, A. Endler, J. Grossmann, W. Gruissem, and S. Baginsky Large-Scale Arabidopsis Phosphoproteome Profiling Reveals Novel Chloroplast Kinase Substrates and Phosphorylation Networks Plant Physiology, June 1, 2009; 150(2): 889 - 903. [Abstract] [Full Text] [PDF]

				N. Yachie, R. Saito, J. Sugahara, M. Tomita, and Y. Ishihama In Silico Analysis of Phosphoproteome Data Suggests a Rich-get-richer Process of Phosphosite Accumulation over Evolution Mol. Cell. Proteomics, May 1, 2009; 8(5): 1061 - 1071. [Abstract] [Full Text] [PDF]

				A. Skirpan, A. H. Culler, A. Gallavotti, D. Jackson, J. D. Cohen, and P. McSteen BARREN INFLORESCENCE2 Interaction with ZmPIN1a Suggests a Role in Auxin Transport During Maize Inflorescence Development Plant Cell Physiol., March 1, 2009; 50(3): 652 - 657. [Abstract] [Full Text] [PDF]

				A. J. Wright, K. Gallagher, and L. G. Smith discordia1 and alternative discordia1 Function Redundantly at the Cortical Division Site to Promote Preprophase Band Formation and Orient Division Planes in Maize PLANT CELL, January 1, 2009; 21(1): 234 - 247. [Abstract] [Full Text] [PDF]

				J. Gao, G. K. Agrawal, J. J. Thelen, and D. Xu P3DB: a plant protein phosphorylation database Nucleic Acids Res., January 1, 2009; 37(suppl_1): D960 - D962. [Abstract] [Full Text] [PDF]

				S. Pajonk, C. Kwon, N. Clemens, R. Panstruga, and P. Schulze-Lefert Activity Determinants and Functional Specialization of Arabidopsis PEN1 Syntaxin in Innate Immunity J. Biol. Chem., October 3, 2008; 283(40): 26974 - 26984. [Abstract] [Full Text] [PDF]

				J. Azimzadeh, P. Nacry, A. Christodoulidou, S. Drevensek, C. Camilleri, N. Amiour, F. Parcy, M. Pastuglia, and D. Bouchez Arabidopsis TONNEAU1 Proteins Are Essential for Preprophase Band Formation and Interact with Centrin PLANT CELL, August 1, 2008; 20(8): 2146 - 2159. [Abstract] [Full Text] [PDF]

				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, May 1, 2008; 1(3): 510 - 527. [Abstract] [Full Text] [PDF]

				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]

				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]

				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]

				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]