Linked Life Data

11389905

Source:http://linkedlifedata.com/resource/pubmed/id/11389905

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-6-6
pubmed:abstractText
The tumor necrosis factor (TNF) inducible protein A20 is a potent inhibitor of nuclear factor-kappaB (IkappaB)-mediated gene expression in response to TNF and several other stimuli. The C-terminal domain of A20 is characterized by seven zinc finger structures. Here, we show that a minimum of four zinc fingers is required to inhibit TNF-induced nuclear factor-kappaB (NF-kappaB) activation to a level that is comparable to that obtained with the wild-type A20 protein. However, there was no strict requirement for a particular zinc finger structure, since a mutant A20 protein containing only the first four zinc fingers was as potent as a mutant protein containing only the last four zinc fingers. A similar functional redundancy of the A20 zinc fingers was also observed for binding of A20 to a number of other proteins, including two novel NF-kappaB inhibitory proteins (ABIN-1, ABIN-2), A20 itself, the anti-apoptotic protein TXBP151, and a regulatory component of the IkappaB kinase complex, IKKgamma. Moreover, we demonstrate that complete loss of binding of any of these proteins correlates with complete loss of A20's ability to inhibit TNF-induced NF-kappaB activation. However, binding of IKKgamma as such is not sufficient for inhibition of NF-kappaB dependent gene expression in response to TNF.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
498
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
93-7
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions.
pubmed:affiliation
Department of Molecular Biology, Unit for Molecular Signal Transduction in Inflammation, University of Ghent, Flanders Interuniversity Institute for Biotechnology, K.L. Ledeganckstraat 35, B-9000 Ghent, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't