Identification and characterization of a novel Rho GTPase activating protein implicated in receptor-mediated endocytosis

Tomohiro Sakakibara, Yasuo Nemoto, Toshihiro Nukiwa, Hiroshi Takeshima

    Research output: Contribution to journalArticlepeer-review

    12 Citations (Scopus)

    Abstract

    Cbl-interacting protein of 85 kDa (CIN85) is a recently identified adaptor protein involved in the endocytic process of several receptor tyrosine kinases. Here we have identified a novel RhoGAP, CIN85 associated multi-domain containing RhoGAP1 (CAMGAP1) as a binding protein for CIN85. CAMGAP1 is composed of an Src homology 3 (SH3) domain, multiple WW domains, a proline-rich region, a PH domain and a RhoGAP domain, and has the domain architecture similar to ARHGAP9 and ARHGAP12. CAMGAP1 mRNA is widely distributed in murine tissues. Biochemical assays showed its GAP activity toward Rac1 and Cdc42. Protein binding and expression studies indicated that the second SH3 domain of CIN85 binds to a proline-rich region of CAMGAP1. Overexpression of a truncated form of CAMGAP1 interferes with the internalization of transferrin receptors, suggesting that CAMGAP1 may play a role in clathrin-mediated endocytosis.

    Original languageEnglish
    Pages (from-to)294-300
    Number of pages7
    JournalFEBS Letters
    Volume566
    Issue number1-3
    DOIs
    Publication statusPublished - 2004 May 21

    Keywords

    • Actin cytoskeleton
    • CHO, Chinese hamster ovary
    • CIN85
    • CIN85, Cbl-interacting protein of 85 kDa
    • Clathrin-mediated endocytosis
    • GAP, GTPase activating protein
    • GST, glutathione S-transferase
    • PH, pleckstrin homology
    • Rho GAP
    • Rho GTPase
    • SH3, Src homology 3

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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