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PubMed · 15135048

SH3P2 in complex with Cbl and Src.

Iwona Szymkiewicz·Olivier Destaing·Pierre Jurdic·Ivan Dikic
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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.

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ActinsAmino Acid MotifsAnimalsCell AdhesionCell LineDNA, ComplementaryFibroblastsFluorescent Antibody Technique, IndirectFocal AdhesionsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMaleMiceModels, BiologicalNIH 3T3 CellsOncogene Protein v-cblOsteoclastsPeptidesPhosphorylationPhosphotyrosinePlasmidsPrecipitin TestsProtein BindingRetroviridae Proteins, OncogenicSpleenTransfectionTwo-Hybrid System TechniquesTyrosinesrc-Family KinasesJournal ArticleResearch Support, Non-U.S. Gov't

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Iwona Szymkiewicz, Olivier Destaing, Pierre Jurdic, Ivan Dikic. 2004-05-07. SH3P2 in complex with Cbl and Src.. https://doi.org/10.1016/j.febslet.2004.03.100

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