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The vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena/VASP-family, regulating actin and cytoskeleton dynamics. Therefore, VASP is an important mediator in processes such as cell-cell adhesion, aggregation, and cellular motility in platelet, fibroblasts, and endothelial cells. The adaptor protein is located at the intersection of two major cyclic nucleotide-dependent signaling pathways, being a substrate of both cAMPand cGMP-dependent kinase. In vitro it is well established that VASP is predominantly phosphorylated at Ser157 and Thr278 residues by cAMPand at Ser239 by cGMPdependent kinase, respectively. In contrast, the detailed cellular functions of distinct VASP phosphorylation(s) in vivo and kinases involved are controversial and are still a matter of debate.

In vivo modulation of vasodilator stimulated phosphoprotein functions by phosphorylation