Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration

Curr Opin Cell Biol. 2002 Feb;14(1):88-103. doi: 10.1016/s0955-0674(01)00299-x.


Actin filament assembly is a tightly regulated process that functions in many aspects of cell physiology. Members of the Ena/VASP (Drosophila Enabled/vasodilator-stimulated phosphoprotein) family are key players in regulating actin filament assembly, in many cases through their association with binding partners that display a particular proline-rich motif, FPPPP. Ena/VASP proteins interact with these partners via the highly conserved Ena/VASP homology 1 (EVH1) domain. The diverse array of binding partners for EVH1 domains, including cytoskeletal proteins such as zyxin, transmembrane guidance receptors such as Roundabout, and the T-cell signaling protein Fyb/SLAP, shows that these interactions are likely to be important in a number of cellular processes that require regulated actin filament assembly.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism
  • Cell Adhesion Molecules / physiology
  • Cell Movement*
  • Cell Polarity*
  • Epithelium / growth & development
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism
  • Microfilament Proteins / physiology*
  • Models, Biological
  • Models, Molecular
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Phosphoproteins / physiology
  • Proline / metabolism
  • Protein Structure, Tertiary


  • Cell Adhesion Molecules
  • Microfilament Proteins
  • Phosphoproteins
  • vasodilator-stimulated phosphoprotein
  • Proline