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This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M700099-MCP200v1 6/11/1980    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 Glossary Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Marmagne, A. Articles by Ephritikhine, G. Search for Related Content PubMed PubMed Citation Articles by Marmagne, A. Articles by Ephritikhine, G. Social Bookmarking                      What's this?

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Research

A High Content in Lipid-modified Peripheral Proteins and Integral Receptor Kinases Features in the Arabidopsis Plasma Membrane Proteome^*,S

Anne Marmagne^,,¶, Myriam Ferro^,||, Thierry Meinnel, Christophe Bruley^||, Lauriane Kuhn^||, Jérome Garin^||, Hélène Barbier-Brygoo and Geneviève Ephritikhine^,**,

From the Institut des Sciences du Végétal, CNRS-UPR 2355, Bât 22, avenue de la Terrasse, 91198 Gif sur Yvette Cedex, France, ^|| Commissariat à l'Energie Atomique, Direction des Sciences du Vivant, Institut de Recherches en Technologies et Sciences pour le Vivant, Laboratoire d'Etude de la Dynamique des Protéomes, INSERM U880, and Université Joseph Fourier, F-38054 Grenoble, France, and ^** Unité de Formation et de Recherche Biologie Sciences de la Nature, Université Paris Diderot Paris 7, 2 place Jussieu, 75251 Paris cedex 05, France

The proteomics of plasma membrane has brought to date only scarce and partial information on the actual protein repertoire. In this work, the plant plasma membrane proteome of Arabidopsis thaliana was investigated. A highly purified plasma membrane fraction was washed by NaCl and Na₂CO₃ salts, and the insoluble fractions were further analyzed by nano-LC-MS/MS. With 446 proteins identified, we hereby describe the largest plasma membrane proteome diversity reported so far. Half of the proteins were predicted to display transmembrane domains and/or to be anchored to the membrane, validating a posteriori the pertinence of the approach. A fine analysis highlighted two main specific and novel features. First, the main functional category is represented by a majority of as yet unreported signaling proteins, including 11% receptor-like kinases. Second, 16% of the identified proteins are predicted to be lipid-modified, specifically involving double lipid linkage through N-terminal myristoylation, S-palmitoylation, C-terminal prenylation, or glycosylphosphatidylinositol anchors. Thus, our approach led for the first time to the identification of a large number of peripheral proteins as part of the plasma membrane and allowed the functionality of the plasma membrane in the cell context to be reconsidered.

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