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J Biol Chem. 2011 Mar 4;286(9):6946-54. doi: 10.1074/jbc.M110.172338. Epub 2010 Dec 23.

Phosphorylation of caspase-8 (Thr-263) by ribosomal S6 kinase 2 (RSK2) mediates caspase-8 ubiquitination and stability.

Author information

1
The Hormel Institute, University of Minnesota, Austin, Minnesota 55912, USA.

Abstract

The ribosomal S6 kinase 2 (RSK2) is a member of the p90 ribosomal S6 kinase (p90RSK) family of proteins and plays a critical role in proliferation, cell cycle, and cell transformation. Here, we report that RSK2 phosphorylates caspase-8, and Thr-263 was identified as a novel caspase-8 phosphorylation site. In addition, we showed that EGF induces caspase-8 ubiquitination and degradation through the proteasome pathway, and phosphorylation of Thr-263 is associated with caspase-8 stability. Finally, RSK2 blocks Fas-induced apoptosis through its phosphorylation of caspase-8. These data provide a direct link between RSK2 and caspase-8 and identify a novel molecular mechanism for caspase-8 modulation by RSK2.

PMID:
21183680
PMCID:
PMC3044950
DOI:
10.1074/jbc.M110.172338
[Indexed for MEDLINE]
Free PMC Article

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