期刊
CANCER CELL
卷 21, 期 5, 页码 694-708出版社
CELL PRESS
DOI: 10.1016/j.ccr.2012.03.040
关键词
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资金
- Leukemia and Lymphoma Society
- National Cancer Institute [P50 CA140158, PO1 CA95426, PO1 CA81534, 1K12 CA133250, RO1 CA107106]
- Harry Mangurian Foundation
- D. Warren Brown Foundation
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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