Vasodilator-stimulated phosphoprotein (VASP)

Vasodilator-stimulated phosphoprotein (VASP) is a cytoskeletal regulatory protein that plays a critical role in the modulation of actin filament dynamics[1][3]. VASP belongs to the Ena/VASP family and links cell signaling pathways to actin dynamics by regulating spatially confined actin filament assembly[3]. Its domain architecture features an N-terminal EVH1 domain for protein interactions, a central proline-rich region, and a C-terminal EVH2 domain responsible for G-actin and F-actin binding as well as tetramerization[1][3]. VASP promotes the elongation and bundling of actin filaments, counteracts capping proteins, facilitates cell migration, and is especially important for lamellipodia and filopodia formation in migrating cells[1][3]. VASP function and localization are regulated by phosphorylation in response to a range of stimuli, reflecting its integration in cellular signaling networks, often downstream of cyclic nucleotide pathways[3]. Dysregulation of VASP has been implicated in cardiovascular diseases as well as cancer cell invasion and metastasis due to its role in cell motility[3]. Currently, VASP itself is not considered a direct therapeutic target or receptor, but it is a significant modulator of cytoskeletal and motility-related processes within cells[1][3].

Other names

Ena/VASP proteinVasodilator stimulated phosphoproteinVASP