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RSK2 mediates NF‐κB activity through the phosphorylation of IκBα in the TNF‐R1 pathway
Author(s) -
Peng Cong,
Cho YongYeon,
Zhu Feng,
Xu YanMing,
Wen Weihong,
Ma WeiYa,
Bode Ann M.,
Dong Zigang
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.09-151290
Subject(s) - ribosomal s6 kinase , phosphorylation , serine , kinase , microbiology and biotechnology , iκbα , tumor necrosis factor alpha , chemistry , threonine , signal transduction , nf κb , biology , endocrinology , p70 s6 kinase 1 , protein kinase b
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 IκBα at Ser‐32, leading to lκBα degradation. The phosphorylation of IκBα 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.—Peng, C., Cho, Y.‐Y., Zhu, F., Xu, Y.‐M., Wen, W., Ma, W.‐Y., Bode, A. M., Dong, Z. RSK2 mediates NF‐κB activity through the phosphorylation of IκBα in the TNF‐R1 pathway. FASEB J . 24, 3490–3499 (2010). www.fasebj.org