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J. Biol. Chem., Vol. 277, Issue 11, 9580-9589, March 15, 2002
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From the Huntsman Cancer Institute and Department of Biology,
University of Utah, Salt Lake City, Utah 84112 and the
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 p130Cas 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.
Members of the Zyxin Family of LIM Proteins Interact with Members
of the p130Cas Family of Signal Transducers*
,, and University of Tokyo, 7-3-1, Hongo, Bunkyo-ku,
Tokyo, 113-8655, Japan
*
This work was supported by National Institutes of Health
Grant GM50877 (to M. C. B.), National Research Service Awards
(to S. K. and S. B.), the Huntsman Cancer Foundation, and the
University of Utah DNA-Peptide Facility and Sequencing Facility
technical support Grant CA42014.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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