SH3P2 is a novel Cbl-interacting protein that participates in regulation of actin dynamics
2004 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 565, no 1-3, 33-38 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
Elsevier B.V. , 2004. Vol. 565, no 1-3, 33-38 p.
Actin; Cbl; Osteoclast; Podosome; SH3; Src
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-90467DOI: 10.1016/j.febslet.2004.03.100PubMedID: 15135048OAI: oai:DiVA.org:uu-90467DiVA: diva2:162830