Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration

Annu Rev Cell Dev Biol. 2003;19:541-64. doi: 10.1146/annurev.cellbio.19.050103.103356.


Ena/VASP proteins are a conserved family of actin regulatory proteins made up of EVH1, EVH2 domains, and a proline-rich central region. They have been implicated in actin-based processes such as fibroblast migration, axon guidance, and T cell polarization and are important for the actin-based motility of the intracellular pathogen Listeria monocytogenes. Mechanistically, these proteins associate with barbed ends of actin filaments and antagonize filament capping by capping protein (CapZ). In addition, they reduce the density of Arp2/3-dependent actin filament branches and bind Profilin at sites of actin polymerization. Vertebrate Ena/VASP proteins are substrates for PKA/PKG serine/threonine kinases. Phosphorylation by these kinases appears to modulate Ena/VASP function within cells, although the mechanism underlying this regulation remains to be determined.

Publication types

  • Review

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actins / metabolism*
  • Animals
  • CapZ Actin Capping Protein
  • Cell Adhesion Molecules / metabolism*
  • Cell Movement / physiology*
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Microfilament Proteins / metabolism
  • Muscle Proteins / metabolism
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Structure, Tertiary / physiology
  • Protein-Serine-Threonine Kinases / metabolism


  • Actins
  • CapZ Actin Capping Protein
  • Cell Adhesion Molecules
  • DNA-Binding Proteins
  • ENA-VASP proteins
  • Microfilament Proteins
  • Muscle Proteins
  • Phosphoproteins
  • vasodilator-stimulated phosphoprotein
  • Protein-Serine-Threonine Kinases