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- Title
RSK2 mediates NF-κB activity through the phosphorylation of IκBα in the TNF-R1 pathway.
- Authors
Peng, Cong; Cho, Yong-Yeon; Zhu, Feng; Xu, Yan-Ming; Wen, Weihong; Ma, Wei-Ya; Bode, Ann M.; Dong, Zigang
- Abstract
The ribosomal S6 kinase 2 (RSK2) is a well-known serine/threonine kinase and a member of the p90 ribosomal S6 kinase (p90RSK) family of proteins. It is activated downstream of the MEK/ERKs cascade by mitogenic stimuli such as EGF or TPA. Here, we show that RSK2 is activated by treatment with tumor necrosis factor-α (TNF-α) and directly phosphorylates IB at Ser-32, leading to IB degradation. The phosphorylation of IB promotes the activation and translocation of the nuclear factor-ΚB (NF-κB) subunits p65 and p50 to the nucleus. The net result is an increased NF-κB activity, which serves as a mechanism for RSK2 blockade of TNF-α-induced apoptosis and enhanced cell survival.
- Subjects
APOPTOSIS; SERINE; COCARCINOGENS; EPIDERMAL growth factor; PHOSPHORYLATION
- Publication
FASEB Journal, 2010, Vol 24, Issue 9, p3490
- ISSN
0892-6638
- Publication type
Article
- DOI
10.1096/fj.09-151290