[PDF][PDF] Tetraspanin CD37 directly mediates transduction of survival and apoptotic signals
R Lapalombella, YY Yeh, L Wang, A Ramanunni… - Cancer cell, 2012 - cell.com
R Lapalombella, YY Yeh, L Wang, A Ramanunni, S Rafiq, S Jha, J Staubli, DM Lucas…
Cancer cell, 2012•cell.comTetraspanins 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" …
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" …
Summary
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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