HEXA encodes the alpha subunit of hexosaminidase A (HexA), a lysosomal enzyme that hydrolyzes N-acetyl-D-hexosamine residues from glycoconjugates, including glycoproteins, neutral glycolipids, and mucopolysaccharides 1234. The HexA isozyme specifically catalyzes GM2 ganglioside degradation in conjunction with the GM2A cofactor, a function unique among hexosaminidase isoforms 234. HEXA mutations cause Tay-Sachs disease (TSD), a lysosomal storage disorder characterized by GM2 ganglioside accumulation in neural cells 5. Both infantile-onset and late-onset TSD variants result from HEXA deficiency, leading to progressive neurological decline and reduced lifespan 67. Recent therapeutic approaches include AAV-mediated gene therapy targeting CNS delivery, which has demonstrated disease stabilization and extended survival in early human trials 6. Genome editing strategies, including prime editing and base editing, show promise for correcting pathogenic HEXA mutations with minimal off-target effects 87. These emerging treatments represent significant advances toward clinical intervention for this previously untreatable lysosomal storage disorder.