Abstract:
:SOCS1 is lost in many human tumors, but its tumor suppression activities are not well understood. We report that SOCS1 is required for transcriptional activity, DNA binding, and serine 15 phosphorylation of p53 in the context of STAT5 signaling. In agreement, inactivation of SOCS1 disabled p53-dependent senescence in response to oncogenic STAT5A and radiation-induced apoptosis in T cells. In addition, SOCS1 was sufficient to induce p53-dependent senescence in fibroblasts. The mechanism of activation of p53 by SOCS1 involved a direct interaction between the SH2 domain of SOCS1 and the N-terminal transactivation domain of p53, while the C-terminal domain of SOCS1 containing the SOCS Box mediated interaction with the DNA damage-regulated kinases ATM/ATR. Also, SOCS1 colocalized with ATM at DNA damage foci induced by oncogenic STAT5A. Collectively, these results add another component to the p53 and DNA damage networks and reveal a mechanism by which SOCS1 functions as a tumor suppressor.
journal_name
Mol Celljournal_title
Molecular cellauthors
Calabrese V,Mallette FA,Deschênes-Simard X,Ramanathan S,Gagnon J,Moores A,Ilangumaran S,Ferbeyre Gdoi
10.1016/j.molcel.2009.09.044subject
Has Abstractpub_date
2009-12-11 00:00:00pages
754-67issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(09)00822-3journal_volume
36pub_type
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