Fucosyltransferases 10, 11. GDP-fucose N-glycan core α1,3-fucosyltransferases (FUT10, FUT11)

Abstract

α-l-Fucose is frequently found at terminal sites on various glycan structures and is essential for the generation of many sugar epitopes, as the well-known human Lewis and ABO histo-blood groups, which constitute important immunological barriers for blood transfusion and tissue transplantation (Cooper et al. 1993; Oriol et al. 1980). Lewis structures as sialyl-Lex (sialyl-CD15) are key elements in leukocyte homing (Lowe 2001) and in extravasation process, thus are essential for lymphocyte maturation (Clarke and Watkins 2000) and natural defense functions (Weston et al. 1992). These H and Lewis structures, sialylated or not, have their expression modified or are reexpressed in various cancers, and some of them are used for cancer marker screening (Moriwaki and Miyoshi 2010). All these terminal α2-fucosyltransferases or α3/4-fucosyltransferases are able to transfer α-l-fucose onto lactosamine-related acceptor substrates. Alternatively, the α6-fucosyltransferase (FUT8) is able to link α-l-fucose onto the innermost core GlcNAc of N-glycans. Another category of enzymes is able to transfer α-l-fucose directly onto the Ser or Thr of glycoproteins. They are called protein-O-fucosyltransferases POFUT1 (FUT12) or POFUT2 (FUT13), and the protein-O-fucosylation of the Notch receptor was found to be essential for its signaling pathway (Stahl et al. 2008).