Linked Life Data

15331758

Source:http://linkedlifedata.com/resource/pubmed/id/15331758

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-11-24
pubmed:abstractText
Retinoic acid receptors (RARs) are hormone-regulated transcription factors that play multiple roles in vertebrate development and differentiation. Three isotypes of RARs, alpha, beta, and gamma, are encoded by distinct genetic loci and possess distinct transcriptional properties. Typically, RARalpha represses target gene transcription in the absence of hormone, whereas RARbeta and gamma fail to repress under these conditions. This inability of RARbeta and RARgamma to repress transcription is due to intramolecular interactions between helix 3 and helix 12 of the hormone binding domains of these isotypes that inhibit corepressor binding while favoring coactivator binding. We report here that the converse ability of RARalpha to repress requires the integrity of the receptor F domain, a domain that maps C-terminal to helix 12, varies in sequence among different nuclear receptors, and is of poorly understood function. The F domain appears to help stabilize helix 12 of RARalpha in a more open position that enhances corepressor binding and inhibits coactivator binding in the absence of hormone. Intriguingly, the RARalpha F domain is isotype autonomous in its function. We speculate that the RARalpha F domain may dock elsewhere on the receptor surface, and this intramolecular interaction may maintain RARalpha helix 12 in an open, repression-competent conformation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2839-53
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Retinoic acid receptor-alpha is stabilized in a repressive state by its C-terminal, isotype-specific F domain.
pubmed:affiliation
Section of Microbiology, Division of Biological Sciences, One Shields Avenue, University of California at Davis, Davis, California 95616, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.