西亚试剂：Tetraspanin CD37 Directly Mediates Transduction of Survival

Tetraspanin CD37 Directly Mediates Transduction of Survival and Apoptotic Signals

Rosa Lapalombella1, Yuh-Ying Yeh1, Liwen Wang2, Asha Ramanunni1, Sarwish Rafiq1, 3, Shruti Jha1, Justin Staubli1, 3, David M. Lucas1, 5, Rajeswaran Mani1, 4, Sarah E.M. Herman1, 3, Amy J. Johnson1, 5, Arletta Lozanski1, Leslie Andritsos1, Jeffrey Jones1, Joseph M. Flynn1, Brian Lannutti10, Peter Thompson11, Paul Algate12, Scott Stromatt12, David Jarjoura6, Xiaokui Mo6, Dasheng Wang5, Ching-Shih Chen1, 5, Gerard Lozanski7, Nyla A. Heerema7, Susheela Tridandapani8, Michael A. Freitas9, 13, Natarajan Muthusamy1, 4, 9, 13, ,   and John C. Byrd

Tetraspanins are commonly believed to act only as molecular facilitators, with no direct role in signal transduction. We herein demonstrate that upon ligation, CD37, a tetraspanin molecule expressed on mature normal and transformed B cells, becomes tyrosine phosphorylated, associates with proximal signaling molecules, and initiates a cascade of events leading to apoptosis. Moreover, we have identified two tyrosine residues with opposing regulatory functions: one lies in the N-terminal domain of CD37 in a predicted ITIM-like motif and mediates SHP1-dependent death, whereas the second lies in a predicted ITAM motif in the C-terminal domain of CD37 and counteracts death signals by mediating phosphatidylinositol 3-kinase-dependent survival.

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