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A more recent version of this article appeared on July 1, 2002
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Submitted on January 30, 2002
Revised on March 11, 2002
Accepted on March 25, 2002
1 Department of Cell Biology, Gesellschaft für Biotechnologische Forschung (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany
2 Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA
* Corresponding author. E-mail address: ase{at}GBF.DE.
The Listeria model system has been essential for the identification and characterisation of key regulators of the actin cytoskeleton such as the Arp2/3 complex and Ena/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.
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