ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (ST6GALNAC2)

ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (ST6GALNAC2) is a transmembrane, Golgi-localized glycosyltransferase enzyme that catalyzes the transfer of sialic acid in an alpha-2,6 linkage, primarily to N-acetylgalactosamine on O-glycan structures (notably on mucin-type O-glycans)[1][4]. This modification terminates O-glycan chain elongation, impacting cell-surface sialylation patterns and thereby influencing cell-cell adhesion, protein targeting, bacterial adhesion, and immune recognition[4]. ST6GALNAC2 is structurally characterized by a GT-A fold typical of the GT29 sialyltransferase family and has a unique substrate specificity[1]. Aberrant expression of ST6GALNAC2 has been linked to cancer progression, with context-dependent roles: it is associated with increased invasion and poor prognosis in colorectal and follicular thyroid cancers, but acts as a metastasis suppressor in breast cancer[3]. Its modulation of cancer cell O-glycome can alter susceptibility to lectin binding and metastatic potential[3]. Known mutations affect its enzymatic properties and, indirectly, cell migration phenotypes[2]. There are currently no specific drugs directly targeting this enzyme, but it represents a potential therapeutic and biomarker target in oncology.

Other names

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2ST6GALNAC2SIAT7BSIATL1STHMST6GalNAcIISIAT7-BST6GalNAIIGalNAc alpha-2,6-sialyltransferase IIST6GalNAc IISThMSialyltransferase 7BSAITL1SIAT7sialyltransferase-like 1

Sialylation inhibition/modulation (theoretical, based on sialylation as mechanism; specific drugs not reported)