The molecular mechanisms underlying activation of the I$\kappa$B 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.
%0 Journal Article
%1 Wajant2011
%A Wajant, Harald
%A Scheurich, Peter
%D 2011
%J FEBS Journal
%K 2011 izi scheuric
%N 6
%P 862--876
%R 10.1111/j.1742-4658.2011.08015.x
%T TNFR1-induced activation of the classical NF-κB pathway
%U https://www.ncbi.nlm.nih.gov/pubmed/21232017
%V 278
%X The molecular mechanisms underlying activation of the I$\kappa$B 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.
%7 2011/01/15
%@ 1742-4658 (Electronic)$\backslash$r1742-464X (Linking)
@article{Wajant2011,
abstract = {The molecular mechanisms underlying activation of the I$\kappa$B 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.},
added-at = {2018-02-01T15:19:43.000+0100},
author = {Wajant, Harald and Scheurich, Peter},
biburl = {https://puma.ub.uni-stuttgart.de/bibtex/23e47b14cdfd127a8a5b3c7a104442bce/cristiano},
doi = {10.1111/j.1742-4658.2011.08015.x},
edition = {2011/01/15},
interhash = {6bf6a6d4992f721385fd181ffe0d45e0},
intrahash = {3e47b14cdfd127a8a5b3c7a104442bce},
isbn = {1742-4658 (Electronic)$\backslash$r1742-464X (Linking)},
issn = {1742464X},
journal = {FEBS Journal},
keywords = {2011 izi scheuric},
number = 6,
pages = {862--876},
pmid = {21232017},
timestamp = {2019-01-17T13:33:28.000+0100},
title = {{TNFR1-induced activation of the classical NF-κB pathway}},
url = {https://www.ncbi.nlm.nih.gov/pubmed/21232017},
volume = 278,
year = 2011
}
