Characterization of the actin binding properties of the vasodilator-stimulated phosphoprotein VASP

FEBS Lett. 1999 May 14;451(1):68-74. doi: 10.1016/s0014-5793(99)00546-3.

Abstract

The vasodilator-stimulated phosphoprotein (VASP) colocalizes with the ends of stress fibers in cell-matrix and cell-cell contacts. We report here that bacterially expressed murine VASP directly interacts with skeletal muscle actin in several test systems including cosedimentation, viscometry and polymerization assays. It nucleates actin polymerization and tightly bundles actin filaments. The interaction with actin is salt-sensitive, indicating that the complex formation is primarily based on electrostatic interactions. Actin binding is confined to the C-terminal domain of VASP (EVH2). This domain, when expressed as a fusion protein with EGFP, associates with stress fibers in transiently transfected cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Actin Cytoskeleton / metabolism*
  • Actins / metabolism*
  • Animals
  • Binding Sites
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Chlorides / metabolism
  • Humans
  • Manganese Compounds / metabolism
  • Mice
  • Microfilament Proteins
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Potassium Chloride / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Sodium Chloride / metabolism
  • Transfection

Substances

  • Actins
  • Cell Adhesion Molecules
  • Chlorides
  • Manganese Compounds
  • Microfilament Proteins
  • Phosphoproteins
  • Recombinant Fusion Proteins
  • vasodilator-stimulated phosphoprotein
  • Sodium Chloride
  • Potassium Chloride
  • manganese chloride