Ena/VASP proteins capture actin filament barbed ends

J Biol Chem. 2008 Apr 11;283(15):9814-9. doi: 10.1074/jbc.M710475200. Epub 2008 Feb 18.

Abstract

Ena/VASP (vasodialator-stimulated protein) proteins regulate many actin-dependent events, including formation of protrusive structures, fibroblast migration, neurite extension, cell-cell adhesion, and Listeria pathogenesis. In vitro, Ena/VASP activities on actin are complex and varied. They promote actin assembly, protect filaments from cappers, bundle filaments, and inhibit filament branching. To determine the mechanisms by which Ena/VASP proteins regulate actin dynamics at barbed ends, we monitored individual actin filaments growing in the presence of VASP and profilin using total internal reflection fluorescence microscopy. Filament growth was unchanged by VASP, but filaments grew faster in profilin-actin and VASP than with profilin-actin alone. Actin filaments were captured directly by VASP-coated surfaces via interactions with growing barbed ends. End-attached filaments transiently paused but resumed growth after becoming bound to the surface via a filament side attachment. Thus, Ena/VASP proteins promote actin assembly by interacting directly with actin filament barbed ends, recruiting profilin-actin, and blocking capping.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Actin Cytoskeleton / chemistry*
  • Actin Cytoskeleton / metabolism
  • Actins / chemistry*
  • Actins / metabolism
  • Animals
  • Cell Adhesion / physiology
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / metabolism
  • Cell Movement / physiology
  • Fibroblasts / metabolism
  • Mice
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism
  • Neurites / metabolism
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism
  • Profilins / chemistry*
  • Profilins / metabolism

Substances

  • Actins
  • Cell Adhesion Molecules
  • Microfilament Proteins
  • Phosphoproteins
  • Profilins
  • vasodilator-stimulated phosphoprotein