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Vol. 13, Issue 7, 2383-2396, July 2002
and
*Department of Cell Biology, Gesellschaft für
Biotechnologische Forschung, D-38124 Braunschweig, Germany; and
The Listeria model system has been essential for the
identification and characterization of key regulators of the actin
cytoskeleton such as the Arp2/3 complex and Ena/vasodilator-stimulated
phosphoprotein (VASP) proteins. Although the role of Ena/VASP proteins
in Listeria motility has been extensively studied,
little is known about the contributions of their domains and
phosphorylation state to bacterial motility. To address these issues,
we have generated a panel of Ena/VASP mutants and, upon expression in
Ena/VASP-deficient cells, evaluated their contribution to Ena/VASP
function in Listeria motility. The proline-rich region,
the putative G-actin binding site, and the Ser/Thr phosphorylation of
Ena/VASP proteins are all required for efficient
Listeria motility. Surprisingly, the interaction of
Ena/VASP proteins with F-actin and their potential ability to form
multimers are both dispensable for their involvement in this process.
Our data suggest that Ena/VASP proteins contribute to
Listeria motility by regulating both the nucleation and
elongation of actin filaments at the bacterial surface.
Department of Biology, Massachusetts Institute of
Technology, Cambridge, Massachusetts 02139
Corresponding author. E-mail address:
ase{at}gbf.de.
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