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FEBS J. 2011 Apr;278(6):862-76. doi: 10.1111/j.1742-4658.2011.08015.x. Epub 2011 Feb 8.

TNFR1-induced activation of the classical NF-κB pathway.

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  • 1Division of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Würzburg, Germany. harald.wajant@mail.uni-wuerzburg.de

Abstract

The molecular mechanisms underlying activation of the IκB kinase (IKK) complex are presumably best understood in the context of tumor necrosis factor (TNF) receptor-1 (TNFR1) signaling. In fact, it seems that most, if not all, proteins relevant for this process have been identified and extensive biochemical and genetic data are available for the role of these factors in TNF-induced IKK activation. There is evidence that protein modification-independent assembly of a core TNFR1 signaling complex containing TNFR1-associated death domain, receptor interacting kinase 1, TNF receptor-associated factor 2 and cellular inhibitor of apoptosis protein 1 and 2 starts a chain of nondegrading ubiquitination events that culminate in the recruitment and activation of IKK complex-stimulating kinases and the IKK complex itself. Here, we sum up the known details of TNFR1-induced IKK activation, address arising contradictions and discuss possible explanations resolving the apparent discrepancies.

© 2011 The Authors Journal compilation © 2011 FEBS.

PMID:
21232017
[PubMed - indexed for MEDLINE]
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