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http://purl.uniprot.org/citations/10769203http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10769203http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10769203http://www.w3.org/2000/01/rdf-schema#comment"Many cell adhesion-dependent processes are regulated by tyrosine phosphorylation. In order to investigate the role of tyrosine phosphorylation of the utrophin-dystroglycan complex we treated suspended or adherent cultures of HeLa cells with peroxyvanadate and immunoprecipitated (beta)-dystroglycan and utrophin from cell extracts. Western blotting of (&bgr;)-dystroglycan and utrophin revealed adhesion- and peroxyvanadate-dependent mobility shifts which were recognised by anti-phospho-tyrosine antibodies. Using maltose binding protein fusion constructs to the carboxy-terminal domains of utrophin we were able to demonstrate specific interactions between the WW, EF and ZZ domains of utrophin and (beta)-dystroglycan by co-immunoprecipitation with endogenous (beta)-dystroglycan. In extracts from cells treated with peroxyvanadate, where endogenous (beta)-dystroglycan was tyrosine phosphorylated, (beta)-dystroglycan was no longer co-immunoprecipitated with utrophin fusion constructs. Peptide 'SPOTs' assays confirmed that tyrosine phosphorylation of (beta)-dystroglycan regulated the binding of utrophin. The phosphorylated tyrosine was identified as Y(892) in the (beta)-dystroglycan WW domain binding motif PPxY thus demonstrating the physiological regulation of the (beta)-dystroglycan/utrophin interaction by adhesion-dependent tyrosine phosphorylation."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.org/dc/terms/identifier"doi:10.1242/jcs.113.10.1717"xsd:string
http://purl.uniprot.org/citations/10769203http://purl.org/dc/terms/identifier"doi:10.1242/jcs.113.10.1717"xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Sudol M."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Sudol M."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"James M."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"James M."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Ottersbach K."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Ottersbach K."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Winder S.J."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Winder S.J."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Ilsley J.L."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Ilsley J.L."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Nuttall A."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Nuttall A."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Tinsley J.M."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/author"Tinsley J.M."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/pages"1717-1726"xsd:string
http://purl.uniprot.org/citations/10769203http://purl.uniprot.org/core/pages"1717-1726"xsd:string