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Originally published In Press as doi:10.1074/jbc.M211566200 on December 22, 2002

J. Biol. Chem., Vol. 278, Issue 9, 7099-7107, February 28, 2003
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Lipid Raft-dependent and -independent Signaling through HLA-DR Molecules*

Marlène BouillonDagger , Youssef El FakhryDagger , Julie GirouardDagger , Hayssam Khalil§, Jacques Thibodeau§||, and Walid MouradDagger **

From the Dagger  Centre de Recherche en Rhumatologie et Immunologie, (CHUL), Département de Médecine, Université Laval, Quebec City, Quebec G1V 4G2, Canada and the § Laboratoire d'Immunologie Moléculaire, Département de Microbiologie et Immunologie, Faculté de Médecine, Université de Montréal, Montreal, Quebec H3C 3J7, Canada

Lipid rafts are plasma membrane microdomains that are highly enriched in signaling molecules and that act as signal transduction platforms for many immune receptors. The involvement of these microdomains in HLA-DR-induced signaling is less well defined. We examined the constitutive presence of HLA-DR molecules in lipid rafts, their possible recruitment into these microdomains, and the role of these microdomains in HLA-DR-induced responses. We detected significant amounts of HLA-DR molecules in the lipid rafts of EBV+ and EBV- B cell lines, monocytic cell lines, transfected HeLa cells, tonsillar B cells, and human monocytes. Localization of HLA-DR in these microdomains was unaffected by the deletion of the cytoplasmic domain of both the alpha  and beta  chains. Ligation of HLA-DR with a bivalent, but not a monovalent, ligand resulted in rapid tyrosine phosphorylation of many substrates, especially Lyn, and activation of ERK1/2 MAP kinase. However, the treatment failed to induce further recruitment of HLA-DR molecules into lipid rafts. The HLA-DR-induced signaling events were accompanied by the induction of cell-cell adhesion that could be inhibited by PTK and Lyn but not ERK1/2 inhibitors. Disruption of lipid rafts by methyl-beta -cyclodextrin (Mbeta CD) resulted in the loss of membrane raft association with HLA-DR molecules, inhibition of HLA-DR-mediated protein tyrosine phosphorylation and cell-cell adhesion. Mbeta CD did not affect the activation of ERK1/2, which was absent from lipid rafts. These results indicate that although all the HLA-DR-induced events studied are dependent on HLA-DR dimerization, some require the presence of HLA-DR molecules in lipid rafts, whereas others do not.

* This work was supported by grants from CIHR, the Arthritis Society of Canada, and the Canadian Arthritis Network.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of a Formation Chercheurs & Aide Recherche studentship.

|| Recipient of a Canadian Institutes for Health Research scholarship.

** Recipient of a scientist award from the Arthritis Society of Canada. To whom correspondence should be addressed: Centre de Recherche en Rhumatologie et Immunologie, CHUL, 2705 boulevard Laurier, T1-49, Quebec City, Quebec G1V 4G2, Canada. Tel.: 418-654-2772; Fax: 418-654-2765; E-mail: Walid.Mourad@crchul.ulaval.ca.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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