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Blood, 1 November 2005, Vol. 106, No. 9, pp. 3074-3081. Prepublished online as a Blood First Edition Paper on June 7, 2005; DOI 10.1182/blood-2004-10-4094. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-10-4094v1 106/9/3074    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Zilber, M.-T. Articles by Gelin, C. Search for Related Content PubMed PubMed Citation Articles by Zilber, M.-T. Articles by Gelin, C. Related Collections Immunobiology Phagocytes Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY MHC class II/CD38/CD9: a lipid-raft–dependent signaling complex in human monocytes Marie-Thérèse Zilber, Niclas Setterblad, Thierry Vasselon, Christelle Doliger, Dominique Charron, Nuala Mooney, and Catherine Gelin From Institut National de la Santé et de la Recherche Médicale (INSERM) U662, and Service Commun d'Imagerie, Institut d'Hématologie, Hôpital SaintLouis, Paris, France. Despite a lack of signaling motifs in their cytoplasmic domain, major histocompatibility complex (MHC) class II molecules trigger a variety of intracellular signals that regulate antigen-presenting cell function. They thus may use associated effector molecules as demonstrated on B cells and dendritic cells. The starting point of this study comes from our previous work, which demonstrated that the ecto-enzyme CD38 is functionally linked to MHC class II molecules. We report that CD38 and human leukocyte antigen-DR (HLA-DR) are functionally and physically associated in lipid rafts microdomains of cellsurface monocytes and that the integrity of these domains is necessary for the HLA-DR and CD38 signaling events. Moreover, we identified the tetraspanin CD9 molecule as a partner of the CD38/HLA-DR complex and demonstrated that HLA-DR, CD38, and CD9 share a common pathway of tyrosine kinase activation in human monocytes. The analysis of conjugate formation between monocytes presenting superantigen and T cells shows the active participation of CD9 and HLA-DR on the monocyte surface. Together, these observations demonstrate the presence of a CD38 and HLA-DR signaling complex within tetraspanin-containing lipid rafts and the functional impact of their molecular partner CD9 in antigen presentation. 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