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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2000-9-21
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pubmed:abstractText |
An androgen receptor (AR) interacting protein was isolated from a HeLa cell complementary DNA library by two-hybrid screening in yeast using the AR DNA and ligand binding domains [amino acids (aa) 481-919] as bait. AR binding of the protein in yeast was dependent on the presence of testosterone or dihydrotestosterone (DHT). The isolated protein is identical to thyroid receptor activator molecule TRAM-1 but lacking aa 1-458. TRAM-1 is a steroid receptor coactivator-3 (SRC-3) subtype. In affinity matrix assays, 35S-labeled TRAM-1 bound the GST-AR ligand binding domain (aa 624-919) and GST-AR N-terminal and DNA binding domains (aa 1-660), but not the GST-AR DNA binding domain (aa 544-634) alone. Coexpression of TRAM-1 increased DHT-dependent AR transactivation 5-fold and constitutive activity of AR (aa 1-660) N-terminal and DNA-binding domains increased 9-fold. Full-length TRAM-1 (aa 1-1424) and the partial (aa 459-1424) were AR and GR coactivators as was SRC-1. In human testis, immunostaining of SRC-3 colocalized with AR in nuclei of Sertoli cells and peritubular myoid cells, indicating it could function as an AR coactivator in these cells. SRC-3 was also present in nuclei of spermatogenic cells where AR was not expressed, suggesting it might also be a coactivator with other nuclear receptors that regulate spermatogenesis.
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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 |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Androgens,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/NCOA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/NCOA3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 1,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 3,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Androgen,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0013-7227
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
141
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3440-50
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10965917-Acetyltransferases,
pubmed-meshheading:10965917-Androgens,
pubmed-meshheading:10965917-Blotting, Western,
pubmed-meshheading:10965917-Cells, Cultured,
pubmed-meshheading:10965917-Glutathione Transferase,
pubmed-meshheading:10965917-Histone Acetyltransferases,
pubmed-meshheading:10965917-Humans,
pubmed-meshheading:10965917-Immunohistochemistry,
pubmed-meshheading:10965917-Male,
pubmed-meshheading:10965917-Nuclear Receptor Coactivator 1,
pubmed-meshheading:10965917-Nuclear Receptor Coactivator 3,
pubmed-meshheading:10965917-Oncogene Proteins,
pubmed-meshheading:10965917-Plasmids,
pubmed-meshheading:10965917-Receptors, Androgen,
pubmed-meshheading:10965917-Seminiferous Tubules,
pubmed-meshheading:10965917-Spermatogenesis,
pubmed-meshheading:10965917-Testis,
pubmed-meshheading:10965917-Trans-Activators,
pubmed-meshheading:10965917-Transcription Factors,
pubmed-meshheading:10965917-Transfection,
pubmed-meshheading:10965917-beta-Galactosidase
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pubmed:year |
2000
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pubmed:articleTitle |
Thyroid receptor activator molecule, TRAM-1, is an androgen receptor coactivator.
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pubmed:affiliation |
The Laboratories for Reproductive Biology, University of North Carolina School of Medicine, Chapel Hill 27599-7500, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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