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Subject | Predicate | Object |
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http://purl.uniprot.org/citations/11724572 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11724572 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11724572 | http://www.w3.org/2000/01/rdf-schema#comment | "beta-Dystroglycan is a ubiquitously expressed integral membrane protein that undergoes tyrosine phosphorylation in an adhesion-dependent manner. However, it remains unknown whether tyrosine-phosphorylated beta-dystroglycan interacts with SH2 domain containing proteins. Here, we show that the tyrosine phosphorylation of beta-dystroglycan is constitutively elevated in v-Src transformed cells. We next reconstituted this phosphorylation event in vivo by transiently coexpressing wild-type c-Src with a fusion protein containing full-length beta-dystroglycan. Our results demonstrate that Src-induced tyrosine phosphorylation of beta-dystroglycan is strictly dependent on the presence of a PPxY motif at its extreme C-terminus. In the nonphosphorylated state, this PPxY motif is normally recognized as a ligand by the WW domain; phosphorylation at this site blocks the binding of certain WW domain containing proteins. Using a GST fusion protein carrying the cytoplasmic tail of beta-dystroglycan, we identified five SH2 domain containing proteins that interact with beta-dystroglycan in a phosphorylation-dependent manner, including c-Src, Fyn, Csk, NCK, and SHC. We localized this binding activity to the PPxY motif by employing a panel of beta-dystroglycan-derived phosphopeptides. In addition, tyrosine phosphorylation of beta-dystroglycan in vivo resulted in the coimmunoprecipitation of the same SH2 domain containing proteins, and this binding event required the beta-dystroglycan C-terminal PPxY motif. We discuss the possibility that tyrosine phosphorylation of the PPxY motif within beta-dystroglycan may act as a regulatory switch to inhibit the binding of certain WW domain containing proteins, while recruiting SH2 domain containing proteins."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi011247r"xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi011247r"xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Bedford M.T."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Bedford M.T."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Lee H."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Lee H."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Sudol M."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Sudol M."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Lisanti M.P."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Lisanti M.P."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Sotgia F."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Sotgia F."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Petrucci T."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/author | "Petrucci T."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/pages | "14585-14592"xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/pages | "14585-14592"xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/title | "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins."xsd:string |
http://purl.uniprot.org/citations/11724572 | http://purl.uniprot.org/core/title | "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins."xsd:string |