ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 (ST6GALNAC4)

ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 (ST6GALNAC4) is a type II membrane-bound enzyme in the glycosyltransferase family 29 that catalyzes the transfer of sialic acid in an alpha-2,6 linkage specifically to the trisaccharide Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc, mainly sialylating glycoproteins and playing a crucial role in glycan structure biosynthesis. It is a key modulator of tumor immunology, producing disialyl-T glycans that act as ligands for Siglecs, thereby contributing to tumor immune evasion and associated with poor prognosis in multiple cancers. ST6GALNAC4's activity and expression are regulated by oncogenic factors like MYC, and it is considered an emerging therapeutic target for cancer immunotherapy and glycoengineering due to its role in cell-surface glycan remodeling and immune checkpoint regulation[1][2][3].

Other names

Sialyltransferase 3CSialyltransferase 7DSIAT3CSIAT7DST6GalNAcIVST6GALNACIVAlpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferaseNeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase IVST6GALNAC4 (most common in literature)

Sialyltransferase inhibition disrupts disialyl-T glycan synthesis, which can reduce tumor cell immune evasion and proliferation. Inhibition of glycosylation modulates TGFβ signaling and impairs downstream oncogenic processes.