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Originally published In Press as doi:10.1074/jbc.M403440200 on June 9, 2004

J. Biol. Chem., Vol. 279, Issue 35, 36277-36286, August 27, 2004
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Lipid Rafts in Higher Plant Cells

PURIFICATION AND CHARACTERIZATION OF TRITON X-100-INSOLUBLE MICRODOMAINS FROM TOBACCO PLASMA MEMBRANE*{boxs}

Sébastien Mongrand{ddagger}§, Johanne Morel¶, Jeanny Laroche{ddagger}, Stéphane Claverol||, Jean-Pierre Carde**, Marie-Andrée Hartmann{ddagger}{ddagger}, Marc Bonneu||, Françoise Simon-Plas¶, René Lessire{ddagger}, and Jean-Jacques Bessoule{ddagger}

From the {ddagger}Laboratoire de Biogenèse Membranaire, FRE 2694-CNRS-Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France, Laboratoire de Phytopharmacie, UMR 692 INRA-Université de Bourgogne 86510, 21065 Cédex Dijon, France, **Institut de Biologie Végétale Moléculaire, UMR 619INRA-Université Bordeaux 1-Université Bordeaux 2, 71 Av. Edouard Bourlaux, B.P. 81, 33883 Villenave d'Ornon Cedex, France, ||Plateforme Génomique Fonctionnelle, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France, and {ddagger}{ddagger}Institut de Biologie Moléculaire des Plantes, UPR-CNRS 2357, 67083 Strasbourg Cedex, France

A large body of evidence from the past decade supports the existence of functional microdomains in membranes of animal and yeast cells, which play important roles in protein sorting, signal transduction, or infection by pathogens. They are based on the dynamic clustering of sphingolipids and cholesterol or ergosterol and are characterized by their insolubility, at low temperature, in nonionic detergents. Here we show that similar microdomains also exist in plant plasma membrane isolated from both tobacco leaves and BY2 cells. Tobacco lipid rafts were found to be greatly enriched in a sphingolipid, identified as glycosylceramide, as well as in a mixture of stigmasterol, sitosterol, 24-methylcholesterol, and cholesterol. Phospho- and glycoglycerolipids of the plasma membrane were largely excluded from lipid rafts. Membrane proteins were separated by one- and two-dimensional gel electrophoresis and identified by tandem mass spectrometry or use of specific antibody. The data clearly indicate that tobacco microdomains are able to recruit a specific set of the plasma membrane proteins and exclude others. We demonstrate the recruitment of the NADPH oxidase after elicitation by cryptogein and the presence of the small G protein NtRac5, a negative regulator of NADPH oxidase, in lipid rafts.

Received for publication, March 29, 2004 , and in revised form, June 8, 2004.

* This work was supported by Conseil Régional d'Aquitaine (to J.-J. B., R. L., S. M., and J. L. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains an additional table.

§ To whom correspondence may be addressed: Laboratoire de Biogenèse Membranaire, FRE 2694-CNRS-Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, BP 33076 Bordeaux Cedex, France. Tel.: 33-5-57-57-14-35; Fax: 33-5-56-51-83-61; E-mail: sebastien.mongrand{at}biomemb.u-bordeaux2.fr.


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