Linked Life Data

10428779

Source:http://linkedlifedata.com/resource/pubmed/id/10428779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1999-9-2
pubmed:abstractText
The Ah receptor (AhR), a soluble cytosolic protein, mediates most of the toxic effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and related environmental contaminants. The mechanism of ligand-mediated AhR activation has been, in part, elucidated. The sequence of events following the binding of the AhR/AhR nuclear translocator protein (ARNT) heterodimer to dioxin response elements has yet to be completely understood. The role of coactivator, RIP140, in the modulation of transcriptional activity of AhR/ARNT heterodimer was examined. RIP140 enhanced TCDD-mediated, dioxin response element-driven reporter gene activity in three cell lines. Co-immunoprecipitation and co-localization assays revealed that RIP140 interacted with AhR, but not with ARNT, both in vitro and in cells. Mapping of the interaction sites revealed that RIP140 was recruited by the AhR transactivation domain via the Q-rich subdomain. The RIP140 domain that interacts with the AhR was mapped to a location between amino acid residues 154 and 350, which is distinct from those involved in estrogen receptor binding. The signature motif, LXXLL, which is responsible for binding of several coactivators to nuclear receptors, is not required for RIP140 binding to AhR. These results demonstrate that the AhR recruits coactivators that are capable of enhancing transcription and, thus, the AhR may compete with steroid receptors for a common coactivator pool. In addition, the data suggest that there are distinct motif(s) for the recruitment of RIP140 to AhR and possibly other non-steroid receptors/transcription factors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22155-64
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs.
pubmed:affiliation
Center for Molecular Toxicology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.