Overview:

VASP or Vasodilator-stimulated phosphoprotein is a member of the Ena-VASP protein family which contains an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions (1). VASP also contains proline-rich domain that bind SH3 and WW domain-containing proteins. VASP is associated with filamentous actin formation and likely plays a key role in cell adhesion and motility. VASP is also involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.

References:

1. Brindle, N P J. et al: The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. 318753-757, 1996.