A Conserved Role for Myosin VII in Adhesion

  1. Gregory Bock Organizer and
  2. Jamie Goode
  1. Margaret A. Titus

Published Online: 7 OCT 2008

DOI: 10.1002/047001766X.ch3

Signalling Networks in Cell Shape and Motility: Novartis Foundation Symposium 269

Signalling Networks in Cell Shape and Motility: Novartis Foundation Symposium 269

How to Cite

Titus, M. A. (2005) A Conserved Role for Myosin VII in Adhesion, in Signalling Networks in Cell Shape and Motility: Novartis Foundation Symposium 269 (eds G. Bock and J. Goode), John Wiley & Sons, Ltd, Chichester, UK. doi: 10.1002/047001766X.ch3

Author Information

  1. Department of Genetics, Cell Biology, and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church St. SE, Minneapolis, MN 55455, USA

Publication History

  1. Published Online: 7 OCT 2008
  2. Published Print: 9 SEP 2005

Book Series:

  1. Novartis Foundation Symposia

Book Series Editors:

  1. Novartis Foundation

ISBN Information

Print ISBN: 9780470011904

Online ISBN: 9780470017661

SEARCH

Keywords:

  • class VII myosins (M7);
  • talin;
  • cell–cell and cell–surface contact;
  • focal adhesion kinase (FAK);
  • interference reflection microscopy (IRM);
  • A GFP-tagged DdM7;
  • DdM7 null mutant;
  • M7 function

Summary

The class VII myosins (M7) are expressed in a wide range of organisms. M7 mutants in mice, zebrafish and Dictyostelium exhibit phenotypes that reveal a role for M7 in adhesion in these highly divergent systems, suggesting a basic conservation of M7 function throughout evolution. M7s are characterized by the presence of two FERM domains in their C-terminal tail region, and deletion of either from the Dictyostelium M7 (DdM7) tail results in loss of function without affecting localization. A search for DdM7 binding partners has revealed that talin, an actin-binding protein that provides a key link between adhesion receptors and the actin cytoskeleton, interacts directly with DdM7. The phenotypes of the DdM7 and talin null mutants are highly similar, suggesting that these two proteins work co-operatively to maintain cell-cell and cell-surface contact and that this interaction may also be conserved throughout evolution.