RSK2 mediates NF-κB activity through the phosphorylation of IκBα in the TNF-R1 pathway

Cong Peng, Yong Yeon Cho, Feng Zhu, Yan Ming Xu, Weihong Wen, Wei-Ya Ma, Ann M. Bode, Zigang Dong

Research output: Contribution to journalArticle

34 Scopus citations

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 IκBα at Ser-32, leading to IκBα 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.

Original languageEnglish (US)
Pages (from-to)3490-3499
Number of pages10
JournalFASEB Journal
Volume24
Issue number9
DOIs
StatePublished - Sep 2010

Keywords

  • Apoptosis
  • Cell survival
  • Serine/threonine kinases
  • Tumor promoter

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