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

Cong Peng, Yong Yeon Cho, Feng Zhu, Jishuai Zhang, Weihong Wen, Yanming Xu, Ke Yao, Wei-Ya Ma, Ann M. Bode, Zigang Dong

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)6946-6954
Number of pages9
JournalJournal of Biological Chemistry
Volume286
Issue number9
DOIs
StatePublished - Mar 4 2011

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