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http://purl.uniprot.org/citations/16895919http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16895919http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16895919http://www.w3.org/2000/01/rdf-schema#comment"To decipher the global network of the epidermal growth factor (EGF) receptor-mediated signaling pathway, a large scale proteomic analysis of tyrosine-phosphorylated proteins was conducted. Here, we focus on characterizing a novel protein, CFBP (CIN85/CD2AP family binding protein), identified in the study. CFBP was found to be phosphorylated at tyrosine 204 upon EGF stimulation, and the CIN85/CD2AP family was identified as a binding partner. A proline-rich motif of CFBP is recognized by one of the three Src-homology 3 domains of CIN85/CD2AP, and the affinity of the interaction is regulated by the tyrosine phosphorylation of CFBP. They co-localize in actinenriched structures, and overexpression of CFBP induced morphological changes with actin reorganization. Furthermore, CFBP accelerated the EGF receptor's down-regulation by facilitating the recruitment of Cbl to the CD2AP/CIN85 complex. Two spliced variants of CFBP lacking either exon 5 or 8 are also expressed, and the variant lacking exon 5 without the proline-rich motif lacks the ability to bind to the CIN85/CD2AP family. The CFBP protein seems to play a key role in the ligand-mediated internalization and down-regulation of the EGF receptor."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m605693200"xsd:string
http://purl.uniprot.org/citations/16895919http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m605693200"xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Murata Y."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Murata Y."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Taniguchi H."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Taniguchi H."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Tashiro K."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Tashiro K."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Konishi H."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Konishi H."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Yamauchi E."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Yamauchi E."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Nabeshi H."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/author"Nabeshi H."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/pages"28919-28931"xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/pages"28919-28931"xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/title"CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP."xsd:string
http://purl.uniprot.org/citations/16895919http://purl.uniprot.org/core/title"CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP."xsd:string