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rdf:type |
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lifeskim:mentions |
umls-concept:C0012899,
umls-concept:C0034804,
umls-concept:C0043393,
umls-concept:C0086418,
umls-concept:C0172237,
umls-concept:C1333357,
umls-concept:C1334043,
umls-concept:C1415344,
umls-concept:C1415345,
umls-concept:C1422218,
umls-concept:C1704735,
umls-concept:C1705468
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pubmed:issue |
26
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pubmed:dateCreated |
2001-6-25
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pubmed:databankReference |
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pubmed:abstractText |
Steroid/nuclear hormone receptors are ligand-dependent transcriptional regulators that control gene expression in a wide array of biological processes. The transcriptional activity of the receptors is mediated by an N-terminal ligand-independent transcriptional activation function AF-1 and a C-terminal ligand-dependent transcriptional activation function AF-2. The nuclear receptor coactivator RAC3 (also known as AIB1/ACTR/pCIP/TRAM-1/SRC-3) is amplified in breast cancer cells, where it forms a complex with estrogen receptor (ER) and enhances AF-2 activity of the receptor. Here, we identify a putative human homologue of the yeast DNA repair and transcriptional regulator MMS19 as a RAC3-interacting protein. The human MMS19 interacts with the N-terminal PAS-A/B domain of RAC3 in vivo and in vitro through a conserved C-terminal domain. Interestingly, the human MMS19 also interacts with estrogen receptors in a ligand-independent manner but not with retinoic acid receptor or thyroid hormone receptor. Overexpression of the interacting domain of hMMS19 strongly inhibits ER-mediated transcriptional activation, indicating a dominant negative activity. In contrast, over expression of the full-length hMMS19 enhances ER-mediated transcriptional activation. We find that hMMS19 stimulates the AF-1 activity of ERalpha, but not the AF-2 activity, suggesting that hMMS19 may be an AF-1-specific transcriptional coactivator of estrogen receptor.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/IFNGR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MET18 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MMS19 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 3,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interferon,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TAF6 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIH,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23962-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11279242-Amino Acid Sequence,
pubmed-meshheading:11279242-Cell Line,
pubmed-meshheading:11279242-Cloning, Molecular,
pubmed-meshheading:11279242-DNA Repair,
pubmed-meshheading:11279242-Fungal Proteins,
pubmed-meshheading:11279242-Humans,
pubmed-meshheading:11279242-Molecular Sequence Data,
pubmed-meshheading:11279242-Nuclear Receptor Coactivator 3,
pubmed-meshheading:11279242-Proteins,
pubmed-meshheading:11279242-Receptors, Estrogen,
pubmed-meshheading:11279242-Receptors, Interferon,
pubmed-meshheading:11279242-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11279242-Sequence Homology, Amino Acid,
pubmed-meshheading:11279242-TATA-Binding Protein Associated Factors,
pubmed-meshheading:11279242-Trans-Activators,
pubmed-meshheading:11279242-Transcription Factor TFIID,
pubmed-meshheading:11279242-Transcription Factor TFIIH,
pubmed-meshheading:11279242-Transcription Factors,
pubmed-meshheading:11279242-Transcription Factors, TFII,
pubmed-meshheading:11279242-Transcriptional Activation,
pubmed-meshheading:11279242-Tumor Cells, Cultured,
pubmed-meshheading:11279242-Two-Hybrid System Techniques,
pubmed-meshheading:11279242-Yeasts
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pubmed:year |
2001
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pubmed:articleTitle |
The human homologue of the yeast DNA repair and TFIIH regulator MMS19 is an AF-1-specific coactivator of estrogen receptor.
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pubmed:affiliation |
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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