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J. Biol. Chem., Vol. 279, Issue 18, 18472-18480, April 30, 2004

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Delineation of the HLA-DR Region and the Residues Involved in the Association with the Cytoskeleton^*

Youssef El Fakhry, Marlène Bouillon, Claire Léveillé, Alexandre Brunet¶, Hayssam Khalil||, Jacques Thibodeau**, and Walid Mourad

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

Whereas the association of major histocompatibility complex (MHC) class II molecules with the cytoskeleton and their recruitment into lipid rafts play a critical role during cognate T/antigen-presenting cell interactions, MHC class II-induced signals, regions, and residues involved in their association and recruitment have not yet been fully deciphered. In this study, we show that oligomerization of HLA-DR molecules induces their association with the cytoskeleton and their recruitment into lipid rafts. The association of oligomerized HLA-DR molecules with the cytoskeleton and their recruitment into lipid rafts occur independently. Furthermore, the association with the cytoskeleton is HLA-DR-specific, since oligomerization of HLA-DP triggers its recruitment only into lipid rafts. HLA-DR molecules devoid of both and cytoplasmic tails did not associate with the cytoskeleton, but their recruitment into lipid rafts was unimpeded. Deletion of either the or cytoplasmic tail did not affect the association of HLA-DR with the cytoskeleton and/or recruitment into lipid rafts. HLA-DR molecules that were devoid of the cytoplasmic chain and that had their cytoplasmic chain replaced with the HLA-DP chain or with a chain in which the residues at positions Gly²²⁶-His²²⁷-Ser²²⁸ were substituted by alanine no longer associated with the cytoskeleton. They were, however, still recruited into lipid rafts. Together, these results support the involvement of different regions of the cytoplasmic tails in the association and the recruitment of HLA-DR into different compartments. The differential behavior of HLA-DP and -DR with respect to their association with the cytoskeleton may explain the previously described difference in their transduced signals.

Received for publication, February 2, 2004 , and in revised form, February 17, 2004.

^* This work was supported by grants from the Arthritis Society of Canada and the Canadian Arthritis Network (to W. M.) and by grants from the Canadian Institutes of Health Research (CIHR) and CRS Inc. (to W. M. and J. 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.

^¶ Supported by studentships from the Fonds pour la Formation de Chercheurs et l'Aide à la Recherche.

^|| Supported by a fellowship award from Canadian Arthritis Network (CAN).

^** Recipient of a CIHR 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 Blvd. Laurier, T1–49, Quebec City, Quebec G1V 4G2, Canada. Tel.: 418-654-2772; Fax: 418-654-2765; E-mail: Walid.Mourad{at}crchul.ulaval.ca.

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