SVBP (small vasohibin binding protein) is a chaperone protein that functions as a critical cofactor enhancing the tubulin carboxypeptidase activity of VASH1 and VASH2 12. The VASH-SVBP complex catalyzes removal of the C-terminal tyrosine residue from α-tubulin, a reversible posttranslational modification essential for regulating microtubule dynamics 2. This detyrosination activity is vital for multiple cellular processes: SVBP regulates mitotic spindle function and accurate chromosome 1 3, supports axon and excitatory synapse formation 4, and influences platelet biogenesis 5. Additionally, SVBP enhances VASH1/VASH2 solubility and secretion 4. Biallelic loss-of-function SVBP variants cause neurodevelopmental disorder characterized by intellectual disability, microcephaly, ataxia, and hypotonia, resulting from impaired tubulin detyrosination and altered microtubule dynamics 64. Missense SVBP mutations present milder phenotypes including hereditary spastic paraplegia associated with cytokinesis failure and premature senescence 7. Recent studies reveal therapeutic potential: SVBP inhibition improves cardiac function in hypertrophic cardiomyopathy models 8 and enhances platelet production 5, suggesting the VASH-SVBP complex represents a targetable pathway for select cardiac and hematologic disorders.