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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.
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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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