VASH2 (vasohibin 2) is a tyrosine carboxypeptidase that removes C-terminal tyrosine residues from α-tubulin, thereby regulating microtubule dynamics and cellular functions 1. The enzyme functions as a heterodimer with SVBP, utilizing a non-canonical Cys-His-Ser catalytic architecture for tyrosine cleavage 1. VASH2-mediated tubulin detyrosination plays critical roles in multiple cellular processes including spindle function, chromosome 1 during mitosis, and regulation of kinesin motor protein binding to microtubules 2. Beyond its enzymatic function, VASH2 exhibits subcellular localization-dependent activities: nuclear VASH2 promotes cell proliferation by facilitating G0/G1 to S phase progression 3, while cytoplasmic VASH2 acts as a pro-angiogenic factor 4. VASH2 is significantly implicated in cancer progression, particularly in lung squamous cell carcinoma and pancreatic ductal adenocarcinoma, where it promotes metastasis, chemoresistance, and tumor angiogenesis 25. In pancreatic cancer, VASH2 facilitates metastasis through multiple mechanisms including enhanced cell migration via tubulin detyrosination, promotion of tumor angiogenesis, and recruitment of myeloid-derived suppressor cells 5. The enzyme represents a promising therapeutic target, with tubulin carboxypeptidase inhibitors showing potential for cancer treatment 26.