Linked Life Data

20065040

Source:http://linkedlifedata.com/resource/pubmed/id/20065040

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-3-2
pubmed:abstractText
Estrogen receptors (ERs) are hormone-regulated transcription factors that regulate key aspects of reproduction and development. ERs are unusual in that they do not typically repress transcription in the absence of hormone but instead possess otherwise cryptic repressive functions that are revealed upon binding to certain hormone antagonists. The roles of corepressors in the control of these aspects of ER function are complex and incompletely understood. We report here that ERs recruit SMRT through an unusual mode of interaction involving multiple contact surfaces. Two surfaces of SMRT, located at the N- and C-terminal domains, contribute to the recruitment of the corepressor to ERs in vitro and are crucial for the corepressor modulation of ER transcriptional activity in cells. These corepressor surfaces contact the DNA binding domain of the receptor, rather than the hormone binding domain previously elucidated for other corepressor/nuclear receptor interactions, and are modulated by the ER's recognition of cognate DNA binding sites. Several additional nuclear receptors, and at least one other corepressor, N-CoR, share aspects of this novel mode of corepressor recruitment. Our results highlight a molecular mechanism that helps explain several previously paradoxical aspects of ER-mediated transcriptional antagonism, which may have a broader significance for an understanding of target gene repression by other nuclear receptors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1098-5549
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1434-45
pubmed:dateRevised
2010-9-2
pubmed:meshHeading
pubmed-meshheading:20065040-Amino Acid Motifs, pubmed-meshheading:20065040-Amino Acid Sequence, pubmed-meshheading:20065040-DNA, pubmed-meshheading:20065040-Estradiol, pubmed-meshheading:20065040-Estrogen Receptor alpha, pubmed-meshheading:20065040-Humans, pubmed-meshheading:20065040-Ligands, pubmed-meshheading:20065040-Molecular Sequence Data, pubmed-meshheading:20065040-Nuclear Receptor Co-Repressor 1, pubmed-meshheading:20065040-Nuclear Receptor Co-Repressor 2, pubmed-meshheading:20065040-PPAR alpha, pubmed-meshheading:20065040-Protein Binding, pubmed-meshheading:20065040-Protein Structure, Tertiary, pubmed-meshheading:20065040-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:20065040-Receptors, Thyroid Hormone, pubmed-meshheading:20065040-Response Elements, pubmed-meshheading:20065040-Transcription, Genetic
pubmed:year
2010
pubmed:articleTitle
Estrogen receptors recruit SMRT and N-CoR corepressors through newly recognized contacts between the corepressor N terminus and the receptor DNA binding domain.
pubmed:affiliation
Department of Microbiology, College of Biological Sciences, University of California at Davis, Davis, California 95616, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural