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

Authors: Sakakibara, T  Nemoto, Y  Nukiwa, T  Takeshima, H 
Citation: Sakakibara T, etal., FEBS Lett 2004 May 21;566(1-3):294-300.
Pubmed: (View Article at PubMed) PMID:15147912
DOI: Full-text: DOI:10.1016/j.febslet.2004.03.101

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 Rho1 (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.


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CRRD Object Information
CRRD ID: 1302833
Created: 2004-10-29
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.