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Cell Cycle. 2011 Mar 15;10(6):879-82. Epub 2011 Mar 15.

Further insights into the mechanism of hypoxia-induced NFκB. [corrected].

Author information

  • 1College of Life Sciences, Wellcome Trust Centre for Gene Regulation and Expression, University of Dundee, Dundee, Scotland, UK.

Erratum in

  • Cell Cycle. 2011 Jun 15;10(12):2041.

Abstract

The cellular response to hypoxia relies on the activation of a specific transcriptional program. Although, most of the attention is focused on the transcription factor HIF, other transcription factors are also activated in hypoxia. We have recently described the mechanism for hypoxia induced NFκB. We have demonstrated the crucial dependency on the IKK complex as well as in the upstream IKK kinase TAK1. TAK1 and IKK activation is dependent upon the calcium calmodulin kinase, CaMK2 and requires Ubc13 as the E2 ubiquitin conjugation enzyme. We report a role for XIAP as the possible E3-ubiquitin ligase for this system. Interestingly, hypoxia induced IKK mediated phosphorylation of IκBα, does not lead to degradation. Hypoxia prevents IκBα de-sumoylation of Sumo-2/3 chains on critical lysine residues, normally required for K-48 linked polyubiquitination. Our results define a novel pathway regulating NFκB activation.

PMID:
21325892
[PubMed - indexed for MEDLINE]
PMCID:
PMC3100871
Free PMC Article

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