The BioGRID Database Seperator
Search
Organism:

J. Biol. Chem. Mar (2002); 277(11):9580-9
Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers.
Yi J, Kloeker S, Jensen CC, Bockholt S, Honda H, Hirai H, Beckerle MC
Huntsman Cancer Institute and Department of Biology, University of Utah, Salt Lake City, Utah 84112 and the University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-8655, Japan.
Abstract: Integrin binding to extracellular matrix proteins induces formation of signaling complexes at focal adhesions. Zyxin co-localizes with integrins at sites of cell-substratum adhesion and is postulated to serve as a docking site for the assembly of multimeric protein complexes involved in regulating cell motility. Recently, we identified a new member of the zyxin family called TRIP6. TRIP6 is localized at focal adhesions and overexpression of TRIP6 slows cell migration. In an effort to define the molecular mechanism by which TRIP6 affects cell migration, the yeast two-hybrid assay was employed to identify proteins that directly bind to TRIP6. This assay revealed that both TRIP6 and zyxin interact with CasL/HEF1, a member of the Cas family. This association is mediated by the LIM region of the zyxin family members and the SH2 domain-binding region of CasL/HEF1. Furthermore, the association between p130(Cas) and the two zyxin family members was demonstrated to occur in vivo by co-immunoprecipitation. Zyxin and Cas family members may cooperate to regulate cell motility.
[PUBMED: 11782456] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
terms and conditions - privacy policy - Osprey Network Visualization System
BioGRID: A General Repository for Interaction Datasets.
Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.