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Published 1 October 2001. doi:10.1083/jcb.200106061
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© The Rockefeller University Press, 0021-9525/2001/10/89 $5.00
The Journal of Cell Biology, Volume 155, Number 1, October 1, 2001 89-100

Article

Pivotal role of VASP in Arp2/3 complex–mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility



Justin Skoble1, Victoria Auerbuch1, Erin D. Goley1, Matthew D. Welch1 and Daniel A. Portnoy1,2

1 Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720
2 School of Public Health, University of California at Berkeley, Berkeley, California 94720

Address correspondence to Daniel A. Portnoy, Dept. of Molecular and Cell Biology, 291 Life Science Addition, University of California at Berkeley, Berkeley, California 94720-3200. Tel.: (510) 643-3925. Fax: (510) 643-6791. E-mail: portnoy{at}uclink4.berkeley.edu

The Listeria monocytogenes ActA protein mediates actin-based motility by recruiting and stimulating the Arp2/3 complex. In vitro, the actin monomer-binding region of ActA is critical for stimulating Arp2/3-dependent actin nucleation; however, this region is dispensable for actin-based motility in cells. Here, we provide genetic and biochemical evidence that vasodilator-stimulated phosphoprotein (VASP) recruitment by ActA can bypass defects in actin monomer-binding. Furthermore, purified VASP enhances the actin-nucleating activity of wild-type ActA and the Arp2/3 complex while also reducing the frequency of actin branch formation. These data suggest that ActA stimulates the Arp2/3 complex by both VASP-dependent and -independent mechanisms that generate distinct populations of actin filaments in the comet tails of L. monocytogenes. The ability of VASP to contribute to actin filament nucleation and to regulate actin filament architecture highlights the central role of VASP in actin-based motility.

Key Words: listeria; actins; cell movement; cytoskeleton; microfilament proteins


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