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Vol. 13, Issue 7, 2533-2546, July 2002
Department of Biology, Massachusetts Institute of Technology,
Cambridge, Massachusetts 02139-4307
The Ena/vasodilator-stimulated phosphoprotein (VASP) protein family
is implicated in the regulation of a number of actin-based cellular
processes, including lamellipodial protrusion necessary for whole cell
translocation. A growing body of evidence derived largely from in vitro
biochemical experiments using purified proteins, cell-free extracts,
and pathogen motility has begun to suggest various mechanistic roles
for Ena/VASP proteins in the control of actin dynamics. Using
complementation of phenotypes in Ena/VASP-deficient cells and
overexpression in normal fibroblasts, we have assayed the function of a
panel of mutants in one member of this family, Mena, by mutating highly
conserved sequence elements found in this protein family. Surprisingly,
deletion of sites required for binding of the actin monomer-binding
protein profilin, a known ligand of Ena/VASP proteins, has no effect on
the ability of Mena to regulate random cell motility. Our analysis
revealed two features essential for Ena/VASP function in cell movement,
cyclic nucleotide-dependent kinase phosphorylation sites and an F-actin
binding motif. Interestingly, expression of the C-terminal EVH2 domain
alone is sufficient to complement loss of Ena/VASP function in random
cell motility.
Online version of this article contains video
material. The online version is available at www.molbiolcell.org.
*
Corresponding author. E-mail address:
fgertler{at}mit.edu.
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