TY - JOUR
T1 - Phosphorylation of caspase-8 (Thr-263) by ribosomal S6 kinase 2 (RSK2) mediates caspase-8 ubiquitination and stability
AU - Peng, Cong
AU - Cho, Yong Yeon
AU - Zhu, Feng
AU - Zhang, Jishuai
AU - Wen, Weihong
AU - Xu, Yanming
AU - Yao, Ke
AU - Ma, Wei-Ya
AU - Bode, Ann M.
AU - Dong, Zigang
PY - 2011/3/4
Y1 - 2011/3/4
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M110.172338
DO - 10.1074/jbc.M110.172338
M3 - Article
C2 - 21183680
AN - SCOPUS:79953214075
SN - 0021-9258
VL - 286
SP - 6946
EP - 6954
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 9
ER -