Ena/VASP Proteins: Regulators of the Actin Cytoskeleton and Cell Migration
Top Cited Papers
- 1 November 2003
- journal article
- review article
- Published by Annual Reviews in Annual Review of Cell and Developmental Biology
- Vol. 19 (1) , 541-564
- https://doi.org/10.1146/annurev.cellbio.19.050103.103356
Abstract
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.Keywords
This publication has 110 references indexed in Scilit:
- Requirement of a Vasodilator-stimulated Phosphoprotein Family Member for Cell Adhesion, the Formation of Filopodia, and Chemotaxis in DictyosteliumJournal of Biological Chemistry, 2002
- Regulation of Vasodilator-stimulated Phosphoprotein Phosphorylation and Interaction with Abl by Protein Kinase A and Cell AdhesionJournal of Biological Chemistry, 2002
- Critical Roles of Phosphorylation and Actin Binding Motifs, but Not the Central Proline-rich Region, for Ena/Vasodilator-stimulated Phosphoprotein (VASP) Function during Cell MigrationMolecular Biology of the Cell, 2002
- Contribution of Ena/VASP Proteins to Intracellular Motility ofListeriaRequires Phosphorylation and Proline-rich Core but Not F-Actin Binding or MultimerizationMolecular Biology of the Cell, 2002
- The N-terminal domain of Homer/Vesl is a new class II EVH1 domainJournal of Molecular Biology, 2001
- Phosphorylation of the Vasodilator-stimulated Phosphoprotein Regulates Its Interaction with ActinJournal of Biological Chemistry, 2000
- Characterization of the Interaction between Zyxin and Members of the Ena/Vasodilator-stimulated Phosphoprotein Family of ProteinsJournal of Biological Chemistry, 2000
- Repulsive Axon GuidanceCell, 2000
- Actin polymerization is induced by Arp 2/3 protein complex at the surface of Listeria monocytogenesNature, 1997
- The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteinsCurrent Biology, 1995