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Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers.


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 ID: 11782456


  • Yi J
  • Kloeker S
  • Jensen CC
  • Bockholt S
  • Honda H
  • Hirai H
  • Beckerle MC


The Journal of biological chemistry

Publication Data

March 15, 2002

Associated Grants

  • Agency: NCI NIH HHS, Id: CA42014
  • Agency: NIGMS NIH HHS, Id: GM50877

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Cell Adhesion
  • Cell Movement
  • Crk-Associated Substrate Protein
  • LIM Domain Proteins
  • Metalloproteins
  • Molecular Sequence Data
  • Phosphoproteins
  • Proteins
  • Rabbits
  • Retinoblastoma-Like Protein p130
  • Transcription Factors
  • Two-Hybrid System Techniques