title: Proteomics of plant detergent-resistant membranes.
abstract: A large body of evidence from the past decade supports the existence, in membrane from animal and yeast cells, of functional microdomains that play important roles in protein sorting, signal transduction, or infection by pathogens. Recent reports demonstrated the presence, in plants, of detergent-resistant fractions isolated from plasma membrane. Analysis of the lipidic composition of this fraction revealed its enrichment in sphingolipids and sterols and depletion in phospho- and glycerolipids as previously observed for animal microdomains. One-dimensional gel electrophoresis experiments indicated that these detergent-resistant fractions are able to recruit a specific set of plasma membrane proteins and exclude others. In the present study, we used mass spectrometry to give an extensive description of a tobacco plasma membrane fraction resistant to solubilization with Triton X-100. This led to the identification of 145 proteins whose functional and physicochemical characteristics were analyzed in silico. Parameters such as isoelectric point, molecular weight, number and length of transmembrane segments, or global hydrophobicity were analyzed and compared with the data available concerning plant plasma membrane proteins. Post-translational modifications, such as myristoylation, palmitoylation, or presence of a glycosylphosphatidylinositol anchor, were examined in relation to the presence of the corresponding proteins in these microdomains. From a functional point of view, this analysis indicated that if a primary function of the plasma membrane, such as transport, seems under-represented in the detergent-resistant fraction, others undergo a significant increase of their relative importance. Among these are signaling and response to biotic and abiotic stress, cellular trafficking, and cell wall metabolism. This suggests that these domains are likely to constitute, as in animal cells, signaling platforms involved in these physiological functions.
authors.affiliation: Laboratoire de Phytopharmacie, Unité Mixte de Recherche (UMR) 692 Institut National de la Recherche Agronomique (INRA)/Ecole Nationale d'Enseignement Supérieur Agronomique de Dijon (ENESAD)/Université de Bourgogne, BP 86510, 21065 Dijon Cedex, France.
authors.forename: Johanne
authors.initials: J
authors.lastname: Morel
authors.forename: Stéphane
authors.initials: S
authors.lastname: Claverol
authors.forename: Sébastien
authors.initials: S
authors.lastname: Mongrand
authors.forename: Fabienne
authors.initials: F
authors.lastname: Furt
authors.forename: Jérôme
authors.initials: J
authors.lastname: Fromentin
authors.forename: Jean-Jacques
authors.initials: JJ
authors.lastname: Bessoule
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Blein
authors.forename: Françoise
authors.initials: F
authors.lastname: Simon-Plas
mesh_terms: D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D002478:Cells, Cultured; D013058:Mass Spectrometry; D021962:Membrane Microdomains / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis* / Q000378:metabolism; D017830:Octoxynol / Q000737:chemistry; D010940:Plant Proteins / Q000032:analysis* / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000502:physiology; D020543:Proteome / Q000032:analysis* / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D014026:Nicotiana / Q000378:metabolism*
chemical_list: D008565:Membrane Proteins; D010940:Plant Proteins; D020543:Proteome; D017830:Octoxynol