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rdf:type |
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lifeskim:mentions |
umls-concept:C0040624,
umls-concept:C0205147,
umls-concept:C0205224,
umls-concept:C0384189,
umls-concept:C1145667,
umls-concept:C1334866,
umls-concept:C1335875,
umls-concept:C1514562,
umls-concept:C1705050,
umls-concept:C1705804,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
46
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pubmed:dateCreated |
2003-11-10
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pubmed:abstractText |
Signal transducer and activator of transcription 5 (STAT5) is a transcription factor that activates prolactin (PRL)-dependent gene expression in the mammary gland. For the activation of its target genes, STAT5 recruits coactivators like p300 and the CREB-binding protein (CBP). In this study we analyzed the function of p300/CBP-associated members of the p160/SRC/NCoA-family in STAT5-mediated transactivation of beta-casein expression. We found that only one of them, NCoA-1, acts as a coactivator for both STAT5a and STAT5b. The two coactivators p300/CBP and NCoA-1 cooperatively enhance STAT5a-mediated transactivation. For NCoA-1-dependent coactivation of STAT5, both the activation domain 1 and the amino-terminal bHLH/PAS domain are required. The amino-terminal region mediates the interaction with STAT5a in cells. A motif of three amino acids in an alpha-helical region of the STAT5a-transactivation domain is essential for the binding of NCoA-1 and for the transcriptional activity of STAT5a. Moreover we observed that NCoA-1 is involved in the synergistic action of the glucocorticoid receptor and STAT5a on the beta-casein promoter. These findings support a model in which STAT5, in concert with the glucocorticoid receptor, recruits a multifunctional coactivator complex to initiate the PRL-dependent transcription.
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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/CREB-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/CREBBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Crebbp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Milk Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NCOA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ncoa1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 1,
http://linkedlifedata.com/resource/pubmed/chemical/Prolactin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucocorticoid,
http://linkedlifedata.com/resource/pubmed/chemical/STAT5 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT5A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/STAT5B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Stat5a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Stat5b protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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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 |
14
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45340-51
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12954634-Amino Acid Motifs,
pubmed-meshheading:12954634-Animals,
pubmed-meshheading:12954634-CREB-Binding Protein,
pubmed-meshheading:12954634-Caseins,
pubmed-meshheading:12954634-Cell Line,
pubmed-meshheading:12954634-Cells, Cultured,
pubmed-meshheading:12954634-Chromatin,
pubmed-meshheading:12954634-DNA-Binding Proteins,
pubmed-meshheading:12954634-Dose-Response Relationship, Drug,
pubmed-meshheading:12954634-HeLa Cells,
pubmed-meshheading:12954634-Histone Acetyltransferases,
pubmed-meshheading:12954634-Humans,
pubmed-meshheading:12954634-Luciferases,
pubmed-meshheading:12954634-Mice,
pubmed-meshheading:12954634-Milk Proteins,
pubmed-meshheading:12954634-Models, Genetic,
pubmed-meshheading:12954634-Nuclear Proteins,
pubmed-meshheading:12954634-Nuclear Receptor Coactivator 1,
pubmed-meshheading:12954634-Plasmids,
pubmed-meshheading:12954634-Precipitin Tests,
pubmed-meshheading:12954634-Prolactin,
pubmed-meshheading:12954634-Promoter Regions, Genetic,
pubmed-meshheading:12954634-Protein Binding,
pubmed-meshheading:12954634-Protein Structure, Tertiary,
pubmed-meshheading:12954634-Receptors, Glucocorticoid,
pubmed-meshheading:12954634-STAT5 Transcription Factor,
pubmed-meshheading:12954634-Trans-Activators,
pubmed-meshheading:12954634-Transcription, Genetic,
pubmed-meshheading:12954634-Transcription Factors,
pubmed-meshheading:12954634-Transcriptional Activation,
pubmed-meshheading:12954634-Transfection,
pubmed-meshheading:12954634-Tumor Suppressor Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL motif in the alpha-helical region of the STAT5 transactivation domain.
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pubmed:affiliation |
Georg-Speyer-Haus, Institute for Biomedical Research, Paul-Ehrlich-Strasse 42-44, 60596 Frankfurt, Germany.
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pubmed:publicationType |
Journal Article
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