Formins and VASPs may co-operate in the formation of filopodia

Biochem Soc Trans. 2005 Dec;33(Pt 6):1256-9. doi: 10.1042/BST20051256.

Abstract

Filopodia are finger-like cell protrusions composed of parallel arrays of actin filaments, which elongate through actin polymerization at their tips. These highly dynamic structures seem to be used by many cell types as sensing organs to explore environmental cues and have been implicated in cell motility as well as in cell-substrate adhesion. Formins are highly conserved multidomain proteins that play important roles in the nucleation of actin and the formation of linear actin filaments, yet their role in filopodia formation has remained poorly defined. The Dictyostelium diaphanous-related formin dDia2 is strongly enriched in filopodia tips. Genetic and biochemical analysis revealed that this protein is important for cell migration and cell adhesion, but most importantly for the formation of filopodia. Recently, we have identified the Dictyostelium VASP (vasodilator-stimulated phosphoprotein) orthologue as a binding partner of dDia2 and provide evidence for a co-operative role of both proteins in filopodia formation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Adhesion / physiology
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Dictyostelium / cytology
  • Dictyostelium / metabolism
  • Humans
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Pseudopodia / metabolism*
  • Pseudopodia / ultrastructure

Substances

  • Cell Adhesion Molecules
  • Dia2 protein, Dictyostelium
  • Microfilament Proteins
  • Phosphoproteins
  • Protozoan Proteins