Alpha-(1,3)-fucosyltransferase VI (FUT6) (FUT6)

Alpha-(1,3)-fucosyltransferase VI (FUT6) is a Golgi-resident glycosyltransferase that transfers fucose from GDP-fucose to specific acceptor glycans in α1,3 linkage, catalyzing the final step in the biosynthesis of the selectin ligand sialyl Lewis X; it is classified among the α1,3-fucosyltransferases with distinct acceptor specificity and is described as a “plasma-type” enzyme that synthesizes sLeX on plasma proteins. FUT6 is encoded by the FUT6 gene in humans and contributes to selectin-mediated cell adhesion and trafficking; in cancer, FUT6 can promote selectin ligand expression and metastatic behavior, including facilitating prostate cancer bone metastasis in preclinical models where inhibition by a fucose mimetic reduces metastasis. In cell therapeutics, recombinant FUT6 with GDP-fucose is applied ex vivo to add sLeX onto hematopoietic stem/progenitor cells and other adoptive cell products, enhancing homing and engraftment via E-selectin interactions; FT-VI and FT-VII both enhance CB HSPC engraftment, though FT-VII additionally fucosylates T/B lymphocytes, which may affect immune effects after transplantation.

Other names

Fucosyltransferase 6α1,3-fucosyltransferase VIAlpha-(1,3)-fucosyltransferase VIPlasma-type α1,3-fucosyltransferase (functional descriptor; synthesizes sLeX on plasma proteins)

Enzymatic transfer of L-fucose from GDP-fucose to acceptor glycans in α1,3-linkage to generate sLeX determinants on glycoproteins/glycolipids, enabling E-selectin binding and promoting adhesion/rolling and tissue homing. Drug inhibition (e.g., by fucose mimetics) reduces sLeX formation and selectin-mediated adhesion/trafficking in cancer models.