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© The Rockefeller University Press, 0021-9525/1999//1549 $5.00
The Journal of Cell Biology, Volume 147, Number 7, , 1999 1549-1560

Molecular Dissection of Zyxin Function Reveals Its Involvement in Cell Motility

^a Department of Biology, University of Utah, Salt Lake City, Utah 84112-5550
^b Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112-5550
Department of Biology, Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112-5550.(801) 581-2175(801) 581-4485

mary.beckerle{at}hci.utah.edu

Spatially controlled actin filament assembly is critical for numerous processes, including the vectorial cell migration required for wound healing, cell- mediated immunity, and embryogenesis. One protein implicated in the regulation of actin assembly is zyxin, a protein concentrated at sites where the fast growing ends of actin filaments are enriched. To evaluate the role of zyxin in vivo, we developed a specific peptide inhibitor of zyxin function that blocks its interaction with -actinin and displaces it from its normal subcellular location. Mislocalization of zyxin perturbs cell migration and spreading, and affects the behavior of the cell edge, a structure maintained by assembly of actin at sites proximal to the plasma membrane. These results support a role for zyxin in cell motility, and demonstrate that the correct positioning of zyxin within the cell is critical for its physiological function. Interestingly, the mislocalization of zyxin in the peptide-injected cells is accompanied by disturbances in the distribution of Ena/VASP family members, proteins that have a well-established role in promoting actin assembly. In concert with previous work, our findings suggest that zyxin promotes the spatially restricted assembly of protein complexes necessary for cell motility.

Key Words: zyxin • -actinin • cell motility • Ena/VASP

© 1999 The Rockefeller University Press

Abbreviation used in this paper: ptK2, Potoroo tridactylis kidney.

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