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International Immunology Advance Access originally published online on April 24, 2006
International Immunology 2006 18(6):951-957; doi:10.1093/intimm/dxl031
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© The Japanese Society for Immunology. 2006. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

LFA-1-dependent lipid raft recruitment of DNAM-1 (CD226) in CD4+ T cell

Jun Shirakawa, Yinan Wang, Satoko Tahara-Hanaoka, Shin-ichiro Honda, Kazuko Shibuya and Akira Shibuya

Department of Immunology, Institute of Basic Medical Sciences, Graduate School of Comprehensive Human Sciences and Center for TARA, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8575, Japan

Correspondence to: A. Shibuya; E-mail: ashibuya{at}md.tsukuba.ac.jp

Upon antigen recognition by the TCR, both the leukocyte adhesion molecules DNAM-1 and leukocyte function-associated antigen-1 (LFA-1) associate with lipid rafts and form peripheral supra-molecular activation clusters that surround central-supra-molecular activation clusters at the immunological synapse. The serine residue in the cytoplasmic tail of DNAM-1 is responsible for this association of DNAM-1 with lipid rafts. The TCR-mediated signal also induces physical association of DNAM-1 with LFA-1, for which the serine phosphorylation of DNAM-1 is also responsible. However, how the serine residue is involved in lipid raft recruitment of DNAM-1 has remained unclear. Here, we show that, although the TCR-mediated signal induced the serine phosphorylation of DNAM-1, DNAM-1 did not associate with lipid rafts in CD4+ T cells derived from mice deficient in LFA-1 expression, indicating that lipid raft recruitment of DNAM-1 depends on LFA-1 expression. These results suggest that the serine phosphorylation of DNAM-1 primarily induces physical association of DNAM-1 with LFA-1, which then takes DNAM-1 into lipid raft compartment.

Keywords: DNAM-1, LFA-1, lipid rafts, T cell activation

Transmitting editor: T. Saito


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