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http://purl.uniprot.org/citations/10722728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10722728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10722728http://www.w3.org/2000/01/rdf-schema#comment"The MSG1 nuclear protein has a strong transcriptional activating activity but does not bind directly to DNA. When cotransfected, MSG1 enhances transcription mediated by the Smad transcription factors in mammalian cells in a manner dependent on ligand-induced Smad hetero-oligomerization. However, the mechanism of this MSG1 effect has been unknown. We now show that MSG1 directly binds to the p300/cAMP-response element-binding protein-binding protein (CBP) transcriptional coactivators, which in turn bind to the Smads, and enhances Smad-mediated transcription in a manner dependent on p300/CBP. The C-terminal transactivating domain of MSG1 is required for binding to p300/CBP and enhancement of Smad-mediated transcription; the viral VP16 transactivating domain could not substitute for it. In the N-terminal region of MSG1, we identified a domain that is necessary and sufficient to direct the specific interaction of MSG1 with Smads. We also found that the Hsc70 heat-shock cognate protein also forms complex with MSG1 in vivo, suppressing both binding of MSG1 to p300/CBP and enhancement of Smad-mediated transcription by MSG1. These results indicate that MSG1 interacts with both the DNA-binding Smad proteins and the p300/CBP coactivators through its N- and C-terminal regions, respectively, and enhances the functional link between Smads and p300/CBP."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.12.8825"xsd:string
http://purl.uniprot.org/citations/10722728http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.12.8825"xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Roberts A.B."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Roberts A.B."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Shioda T."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Shioda T."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Isselbacher K.J."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Isselbacher K.J."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Yahata T."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Yahata T."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"de Caestecker M.P."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"de Caestecker M.P."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Andriole S."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Andriole S."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Lechleider R.J."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/author"Lechleider R.J."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/pages"8825-8834"xsd:string
http://purl.uniprot.org/citations/10722728http://purl.uniprot.org/core/pages"8825-8834"xsd:string