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http://purl.uniprot.org/citations/12604611http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12604611http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12604611http://www.w3.org/2000/01/rdf-schema#comment"The multifunctional DNA- and RNA-associated Y-box protein 1 (YB-1) specifically binds to splicing recognition motifs and regulates alternative splice site selection. Here, we identify the arginine/serine-rich SRp30c protein as an interacting protein of YB-1 by performing a two-hybrid screen against a human mesangial cell cDNA library. Co-immunoprecipitation studies confirm a direct interaction of tagged proteins YB-1 and SRp30c in the absence of RNA via two independent protein domains of YB-1. A high affinity interaction is conferred through the N-terminal region. We show that the subcellular YB-1 localization is dependent on the cellular SRp30c content. In proliferating cells, YB-1 localizes to the cytoplasm, whereas FLAG-SRp30c protein is detected in the nucleus. After overexpression of YB-1 and FLAG-SRp30c, both proteins are co-localized in the nucleus, and this requires the N-terminal region of YB-1. Heat shock treatment of cells, a condition under which SRp30c accumulates in stress-induced Sam68 nuclear bodies, abrogates the co-localization and YB-1 shuttles back to the cytoplasm. Finally, the functional relevance of the YB-1/SRp30c interaction for in vivo splicing is demonstrated in the E1A minigene model system. Here, changes in splice site selection are detected, that is, overexpression of YB-1 is accompanied by preferential 5' splicing site selection and formation of the 12 S isoform."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m212518200"xsd:string
http://purl.uniprot.org/citations/12604611http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m212518200"xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Raffetseder U."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Raffetseder U."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Jansen P.L."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Jansen P.L."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Rauen T."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Rauen T."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Frye B."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Frye B."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Juerchott K."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Juerchott K."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Mertens P.R."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Mertens P.R."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Royer H.-D."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/author"Royer H.-D."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/pages"18241-18248"xsd:string
http://purl.uniprot.org/citations/12604611http://purl.uniprot.org/core/pages"18241-18248"xsd:string