The vasodilator-stimulated phosphoprotein (VASP) is a major substrate for cyclic nucleotide-
dependent kinases in platelets and other cardiovascular cells. It promotes actin nucleation
and binds to actin filaments in vitro and associates with stress fibers in cells. The VASP-actin
interaction is salt-sensitive, arguing for electrostatic interactions. Hence, phosphorylation
may significantly alter the actin binding properties of VASP. This hypothesis was
investigated by analyzing complex formation of recombinant murine VASP with actin after …