VASP (vasodilator-stimulated phosphoprotein), is involved in the maintenance of cytoarchitecture by interacting with actin-like filaments. VASP shares a limited degree of homology with the amino terminus of WASP, which is frequently mutated in 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 a protein of between 46 and 50 kDa that is highly expressed in human platelets and, like WASP, may play a role in cytoskeletal organization.