Linked Life Data

19270718

Source:http://linkedlifedata.com/resource/pubmed/id/19270718

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-4-1
pubmed:abstractText
The nuclear factor-kappaB (NF-kappaB) transcription factor system is a crucial component that controls several important biological functions, thus raising the need for mechanisms that ensure the correct termination of its activity. Here, we identify a new phosphorylation/ubiquitination switch in the NF-kappaB network that controls the stability of the transactivating p65 subunit. Tumour necrosis factor-induced phosphorylation of p65 at Ser468 allows binding of COMMD1 and cullin 2, components of a multimeric ubiquitin ligase complex mediating p65 ubiquitination. Mutation of p65 at Ser468 largely prevents p65 ubiquitination and proteasomal degradation. Inducible p65 elimination is restricted to a subset of NF-kappaB target genes such as Icam1. Accordingly, chromatin immunoprecipitation experiments reveal the selective recruitment of Ser468-phosphorylated p65 and COMMD1 to the Icam1 promoter. Phosphorylation of p65 at Ser468 leads to ubiquitin/proteasome-dependent removal of chromatin-bound p65, thus contributing to the selective termination of NF-kappaB-dependent gene expression.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-12360211, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-12482991, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-14690596, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-15226358, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-15465828, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-15809659, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-15837794, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-15858576, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-16046471, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-16407239, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-16982211, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-17183367, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-17468759, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-17561400, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-17673665, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-17908789, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-18267068, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-18443042, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-7931077, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-9500443, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-9660950, http://linkedlifedata.com/resource/pubmed/commentcorrection/19270718-9859996
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1469-3178
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
381-6
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Phosphorylation of NF-kappaB p65 at Ser468 controls its COMMD1-dependent ubiquitination and target gene-specific proteasomal elimination.
pubmed:affiliation
Institute of Biochemistry, Medical Faculty, Friedrichstrasse 24, Justus-Liebig-University, D-35392 Giessen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't