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http://purl.uniprot.org/citations/20398064http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20398064http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20398064http://www.w3.org/2000/01/rdf-schema#comment"Post-translational modification of protein tyrosine phosphatases (PTPs) is implicated in functional modulation of these enzymes. Stomach cancer-associated protein tyrosine phosphatase-1 (SAP-1), as well as protein tyrosine phosphatase receptor type O (PTPRO) and vascular endothelial-protein tyrosine phosphatase (VE-PTP) are receptor-type PTPs (RPTPs), which belong to the R3 subtype RPTP family. Here, we have shown that the carboxyl (COOH)-terminal region of SAP-1 undergoes tyrosine phosphorylation by the treatment with a PTP inhibitor. Src family kinases are important for the tyrosine phosphorylation of SAP-1. Either Grb2 or Fyn, through their Src homology-2 domains, bound to the tyrosine-phosphorylated SAP-1. Moreover, both PTPRO and VE-PTP underwent tyrosine phosphorylation in their COOH-terminal regions. Tyrosine phosphorylation of VE-PTP or PTPRO also promoted their complex formations with Grb2 or Fyn. Forced expression of SAP-1, PTPRO or VE-PTP promoted cell spreading and lamellipodium formation of fibroblasts that expressed an activated form of Ras. In contrast, such effects of non-tyrosine-phosphorylated forms of these RPTPs were markedly smaller than those of wild-type RPTPs. Our results thus suggest that tyrosine phosphorylation of R3 subtype RPTPs promotes their complex formations with Grb2 or Fyn and thus participates in the regulation of cell morphology."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2443.2010.01398.x"xsd:string
http://purl.uniprot.org/citations/20398064http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2443.2010.01398.x"xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Murata Y."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Murata Y."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Mori M."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Mori M."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Kotani T."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Kotani T."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Ohnishi H."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Ohnishi H."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Okazawa H."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Okazawa H."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Kusakari S."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Kusakari S."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Matozaki T."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Matozaki T."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Supriatna Y."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/author"Supriatna Y."xsd:string
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20398064http://purl.uniprot.org/core/date"2010"xsd:gYear