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Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. VASP shares a limited degree of homology with the amino terminus of WASP, which is frequently mutated in Wiskott-Aldrich syndrome (WAS) patients. An established substrate of cAMP and cGMP dependent kinases, VASP is phosphorylated on a regulatory serine residue 157 and localizes to focal adhesions, microfilaments and highly active regions of the plasma membrane. VASP is highly expressed in human platelets and, like WASP, may play a role in cytoskeletal organization.