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- W65105544 abstract "In this report, we describe SH3P2, an SH3-domain containing protein, as a novel Cbl-interacting molecule that is a substrate of tyrosine kinase Src. We identified a specific polyproline motif of Cbl responsible for binding of SH3P2 and Src, and observed mutual sequestration of Src and SH3P2 from monomer Cbl molecules. In adherent cells, SH3P2 associated with Cbl and fibrilar actin and was localized at focal contacts in fibroblasts as well as at the apical part of podosome rings in differentiated osteoclasts. Our data implicate that SH3P2, a novel component of adhesion sites, is involved in Cbl and Src-mediated pathways." @default.
- W65105544 created "2016-06-24" @default.
- W65105544 creator A5039122115 @default.
- W65105544 date "2003-01-01" @default.
- W65105544 modified "2023-09-23" @default.
- W65105544 title "Cbl in Regulation of Growth Factor Receptor Endocytosis and Actin Dynamics" @default.
- W65105544 hasPublicationYear "2003" @default.
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