VASH1 is a tyrosine carboxypeptidase that removes the C-terminal tyrosine residue from α-tubulin, thereby regulating microtubule dynamics 12. This detyrosination activity is critical for spindle function and accurate chromosome 14 during mitosis 2. VASH1 functions as a potent angiogenesis inhibitor, selectively suppressing endothelial cell migration, proliferation, and network formation without affecting smooth muscle cells or fibroblasts 34. Beyond angiogenesis, VASH1 has emerged as a multifunctional regulator with therapeutic potential across diverse pathologies. In cardiovascular disease, VASH1 inhibition reduces myocardial stiffness and improves diastolic relaxation in heart failure with preserved ejection fraction models, suggesting a novel therapeutic approach 5. In ocular pathology, VASH1 suppresses endothelial-to-mesenchymal transition in age-related macular degeneration through the circSIRT2/miR-542-3p/VASH1 regulatory axis 6. VASH1 detyrosination activity is essential for proper platelet biogenesis, with VASH1-SVBP identified as the predominant detyrosinase in the megakaryocyte lineage 7. In renal function, VASH1 maintains glomerular filtration barrier integrity through α-tubulin detyrosination in podocytes 8. Paradoxically, elevated VASH1 expression correlates with poor prognosis in multiple cancers, including ovarian and gastroenterological malignancies, where it exhibits tumor-suppressive properties 910. These findings establish VASH1 as a key regulator of the tubulin code with broad clinical implications.