Fucosyltransferase 6 (FUT6)

Fucosyltransferase 6 (FUT6) is a Golgi-associated type II transmembrane enzyme that catalyzes the transfer of L-fucose from GDP-fucose donors to N-acetylglucosamine (GlcNAc) residues of glycoproteins and glycolipids, specifically forming an alpha-1,3 glycosidic linkage essential for the biosynthesis of sialyl-Lewis X (sLe^x^), which serves as a ligand for E-selectin and is important in leukocyte adhesion and trafficking[1][5]. FUT6 belongs to the family of alpha-1,3-fucosyltransferases, which share a high degree of sequence homology and are involved in synthesizing complex Lewis antigen structures[5]. Mutations in FUT6 cause fucosyltransferase-6 deficiency, leading to altered glycan expression and associated clinical phenotypes including rare cases of metabolic syndrome[1]. Overexpression or altered activity of FUT6 is implicated in various cancers by modulating cell adhesion, migration, and immune evasion through altered surface glycans[1][3][5]. FUT6 is mainly studied as a potential therapeutic target and biomarker in cancer and immune-related conditions, but currently, there are no approved drugs targeting this enzyme directly in the clinic[1][5].

Other names

Alpha-(1,3)-fucosyltransferaseFuc-TVIFuc-T6CD15s synthaseLewis X synthase

Inhibition of FUT6 can reduce cell-cell adhesion and block formation of sialyl-Lewis X, potentially impacting leukocyte migration and metastasis[1][5].