VASP (vasodilator-stimulated phosphoprotein) is a 39-kDa actin-binding protein that functions as an 'anti-capping' protein antagonizing capping proteins at actin filament barbed ends 1. VASP promotes actin filament elongation by facilitating profilin-bound actin monomer transfer to growing filament ends and localizes to focal adhesions, filopodial tips, and the lamellipodial leading edge 2. Through its proline-rich central domain, VASP recruits profilin and binds focal adhesion proteins vinculin and zyxin, directing local actin assembly during cell migration 2. VASP is phosphorylated at multiple sites by kinases including Abl, PKA, PKG, and AMPK, with phosphorylation regulating both actin dynamics and cellular localization 3. In disease contexts, VASP is significantly upregulated in hepatocellular carcinoma and breast cancer, where elevated expression correlates with poor prognosis, advanced pathological stage, and aggressive phenotypes 45. In hepatocellular carcinoma, hypoxia-induced VASP upregulation promotes migration and invasion through AKT/ERK signaling and EMT activation via HIF-1α, miR-204, and TGF-β pathways 4. Functionally, VASP knockdown significantly reduces breast cancer cell migration and proliferation 5. VASP also regulates platelet aggregation by inhibiting filament disassembly during shape transformation 6 and participates in podocyte function and glomerular filtration barrier integrity 3.