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http://purl.uniprot.org/citations/12954634http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12954634http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12954634http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m303644200"xsd:string
http://purl.uniprot.org/citations/12954634http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m303644200"xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Pfitzner E."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Pfitzner E."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Litterst C.M."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Litterst C.M."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Kliem S."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Kliem S."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Marilley D."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/author"Marilley D."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/pages"45340-45351"xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/pages"45340-45351"xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/title"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."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/title"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."xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12954634http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12954634http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12954634
http://purl.uniprot.org/citations/12954634http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12954634