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http://purl.uniprot.org/citations/11390389http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11390389http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11390389http://www.w3.org/2000/01/rdf-schema#comment"Phospholipid scramblase 1 (PLSCR1) is a plasma membrane protein that has been proposed to play a role in the transbilayer movement of plasma membrane phospholipids. PLSCR1 contains multiple proline-rich motifs resembling Src homology 3 (SH3) domain-binding sites. An initial screen against 13 different SH3 domains revealed a marked specificity of PLSCR1 for binding to the Abl SH3 domain. Binding between intracellular PLSCR1 and c-Abl was demonstrated by co-immunoprecipitation of both proteins from several cell lines. Deletion of the proline-rich segment in PLSCR1 (residues 1--118) abolished its binding to the Abl SH3 domain. PLSCR1 was Tyr-phosphorylated by c-Abl in vitro. Phosphorylation was abolished by mutation of Tyr residues Tyr(69)/Tyr(74) within the tandem repeat sequence (68)VYNQPVYNQP(77) of PLSCR1, implying that these residues are the likely sites of phosphorylation. Cellular PLSCR1 was found to be constitutively Tyr-phosphorylated in several cell lines. The Tyr phosphorylation of PLSCR1 was increased upon overexpression of c-Abl and significantly reduced either upon cell treatment with the Abl kinase inhibitor STI571, or in Abl-/-mouse fibroblasts, suggesting that cellular PLSCR1 is a normal substrate of c-Abl. Cell treatment with the DNA-damaging agent cisplatin activated c-Abl kinase and increased Tyr phosphorylation of PLSCR1. The cisplatin-induced phosphorylation of PLSCR1 was inhibited by STI571 and was not observed in Abl-/-fibroblasts. These findings indicate that c-Abl binds and phosphorylates PLSCR1, and raise the possibility that an interaction between c-Abl and plasma membrane PLSCR1 might contribute to the cellular response to genotoxic stress."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m102505200"xsd:string
http://purl.uniprot.org/citations/11390389http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m102505200"xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Sun J."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Sun J."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Zhao J."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Zhao J."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Wang J.Y."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Wang J.Y."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Sims P.J."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Sims P.J."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Schwartz M.A."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Schwartz M.A."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Wiedmer T."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/author"Wiedmer T."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/pages"28984-28990"xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/pages"28984-28990"xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/title"c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1."xsd:string
http://purl.uniprot.org/citations/11390389http://purl.uniprot.org/core/title"c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1."xsd:string