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

Justin Skoble, Victoria Auerbuch, Erin D. Goley, Matthew D. Welch, Daniel A. Portnoy

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)89-100
Number of pages12
JournalJournal of Cell Biology
Volume155
Issue number1
DOIs
StatePublished - Oct 1 2001
Externally publishedYes

Keywords

  • Actins
  • Cell movement
  • Cytoskeleton
  • Listeria
  • Microfilament proteins

ASJC Scopus subject areas

  • Cell Biology

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