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Article
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
Women’s Health Research Faculty Publications
  • Norio Takizawa, University of Massachusetts Medical School
  • Tara C. Smith, University of Massachusetts Medical School
  • Thomas Nebl, University of Massachusetts Medical School
  • Jessica Lynn Crowley, University of Massachusetts Medical School
  • Stephen J. Palmieri
  • Lawrence M. Lifshitz, University of Massachusetts Medical School
  • Anka G. Ehrhardt, University of Massachusetts Medical School
  • Laura M. Hoffman
  • Mary C. Beckerle
  • Elizabeth J. Luna, University of Massachusetts Medical School
UMMS Affiliation
Department of Cell Biology; Department of Physiology; Program in Molecular Medicine
Date
8-2-2006
Document Type
Article
Subjects
Adaptor Proteins, Signal Transducing; Animals; COS Cells; Cattle; Cells, Cultured; Cercopithecus aethiops; Down-Regulation; Focal Adhesions; Green Fluorescent Proteins; Humans; Membrane Proteins; Mice; Microfilament Proteins; Microtubule-Associated Proteins; Myocytes, Smooth Muscle; Nuclear Proteins; Protein Binding; Rats; Regulatory Sequences, Nucleic Acid; Transcription Factors
Abstract

Cell-substrate contacts, called focal adhesions (FAs), are dynamic in rapidly moving cells. We show that supervillin (SV)--a peripheral membrane protein that binds myosin II and F-actin in such cells--negatively regulates stress fibers, FAs, and cell-substrate adhesion. The major FA regulatory sequence within SV (SV342-571) binds to the LIM domains of two proteins in the zyxin family, thyroid receptor-interacting protein 6 (TRIP6) and lipoma-preferred partner (LPP), but not to zyxin itself. SV and TRIP6 colocalize within large FAs, where TRIP6 may help recruit SV. RNAi-mediated decreases in either protein increase cell adhesion to fibronectin. TRIP6 partially rescues SV effects on stress fibers and FAs, apparently by mislocating SV away from FAs. Thus, SV interactions with TRIP6 at FAs promote loss of FA structure and function. SV and TRIP6 binding partners suggest several specific mechanisms through which the SV-TRIP6 interaction may regulate FA maturation and/or disassembly.

Rights and Permissions
Citation: J Cell Biol. 2006 Jul 31;174(3):447-58. Link to article on publisher's site
Related Resources
Link to article in PubMed
PubMed ID
16880273
Citation Information
Norio Takizawa, Tara C. Smith, Thomas Nebl, Jessica Lynn Crowley, et al.. "Supervillin modulation of focal adhesions involving TRIP6/ZRP-1" Vol. 174 Iss. 3 (2006) ISSN: 0021-9525 (Print)
Available at: http://works.bepress.com/lunae/10/