Fucosyltransferases 10, 11. GDP-Fucose N-Glycan Core α1,3-Fucosyltransferases (FUT10, FUT11)

  • Rosella MolliconeEmail author
  • Rafael Oriol
Reference work entry


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).


Acceptor Substrate Endoplasmic Reticulum Retention Signal Lewis Structure Endoplasmic Reticulum Resident Terminal GlcNAc 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. Aalberse RC, Koshte V, Clemens JG (1981) Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom. J Allergy Clin Immunol 68:356–364PubMedCrossRefGoogle Scholar
  2. Altmann F (2007) The role of protein glycosylation in allergy. Int Arch Allergy Immunol 142:99–115PubMedCrossRefGoogle Scholar
  3. Baboval T, Smith FI (2002) Comparison of human and mouse Fuc-TX and Fuc-TXI genes, and expression studies in the mouse. Mamm Genome 13:538–541PubMedCrossRefGoogle Scholar
  4. Bakker H, Schijlen E, de Vries T, Schiphorst WE, Jordi W, Lommen A, Bosch D, van Die I (2001) Plant members of the α1,3/4-fucosyltransferase gene family encode an α1,4-fucosyltransferase, potentially involved in Lewis(a) biosynthesis, and two core α1,3-fucosyltransferases. FEBS Lett 507:307–312PubMedCrossRefGoogle Scholar
  5. Both P, Sobczak L, Breton C, Hann S, Nobauer K, Paschinger K, Kozmon S, Mucha J, Wilson IB (2011) Distantly related plant and nematode core α1,3-fucosyltransferases display similar trends in structure-function relationships. Glycobiology 21:1401–1415PubMedCentralPubMedCrossRefGoogle Scholar
  6. Breton C, Oriol R, Imberty A (1998) Conserved structural features in eukaryotic and prokaryotic fucosyltransferases. Glycobiology 8:87–94PubMedCrossRefGoogle Scholar
  7. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:D233–D238PubMedCentralPubMedCrossRefGoogle Scholar
  8. Clarke JL, Watkins WM (2000) α1,3-l-fucosyltransferase expression in the developing human myeloid cells. Antigenic, enzymatic and mRNA analysis. J Biol Chem 271:10317–10328Google Scholar
  9. Cooper DK, Ye Y, Niekrasz M, Kehoe M, Martin M, Neethling FA, Kosanke S, DeBault LE, Worsley G, Zuhdi N et al. (1993) Specific intravenous carbohydrate therapy. A new concept in inhibiting antibody-mediated rejection-experience with ABO-incompatible cardiac allografting in the baboon. Transplantation 56:769–777PubMedCrossRefGoogle Scholar
  10. Dupuy F, Petit JM, Mollicone R, Oriol R, Julien R, Maftah A (1999) A single amino acid in the hypervariable stem domain of vertebrate α1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer. Characterization of acceptor substrate specificity of the Lewis enzyme by site-directed mutagenesis. J Biol Chem 274:12257–12262PubMedCrossRefGoogle Scholar
  11. Fabini G, Freilinger A, Altmann F, Wilson IBH (2001) Identification of core α1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster – Potential basis of the neural anti-horseradish peroxidase epitope. J Biol Chem 276:28058–28067PubMedCrossRefGoogle Scholar
  12. Groux-Degroote S, Krzewinski-Recchi MA, Cazet A, Vincent A, Lehoux S, Lafitte JJ, Van Seuningen I, Delannoy P (2008) IL-6 and IL-8 increase the expression of glycosyltransferases and sulfotransferases involved in the biosynthesis of sialylated and/or sulfated Lewisx epitopes in the human bronchial mucosa. Biochem J 410:213–223PubMedCrossRefGoogle Scholar
  13. Hemmer W, Focke M, Kolarich D, Wilson IB, Altmann F, Wohrl S, Gotz M, Jarisch R (2001) Antibody binding to venom carbohydrates is a frequent cause for double positivity to honeybee and yellow jacket venom in patients with stinging-insect allergy. J Allergy Clin Immunol 108:1045–1052PubMedCrossRefGoogle Scholar
  14. Leiter H, Mucha J, Staudacher E, Grimm R, Glössl J, Altmann F (1999) Purification, cDNA cloning, and expression of GDP-l-Fuc: Asn-linked GlcNAc α1,3-fucosyltransferase from mung beans. J Biol Chem 274:21830–21839PubMedCrossRefGoogle Scholar
  15. Lowe JB (2001) Glycosylation, immunity, and autoimmunity. Cell 104:809–812PubMedCrossRefGoogle Scholar
  16. Luo Y, Haltiwanger RS (2005) O-fucosylation of Notch occurs in the endoplasmic reticulum. J Biol Chem 280:11289–11294PubMedCrossRefGoogle Scholar
  17. Martinez-Duncker I, Michalski JC, Bauby C, Candelier JJ, Mennesson B, Codogno P, Oriol R, Mollicone R (2004) Activity and tissue distribution of splice variants of α6-fucosyltransferase in human embryogenesis. Glycobiology 14:13–25PubMedCrossRefGoogle Scholar
  18. Mollicone R, Moore S, Bovin N, Garcia-Rosasco M, Candelier J, Martinez-Dunker I, Oriol R (2009) Activity, splice variants, conserved peptide motifs, and phylogeny of two new α1,3-fucosyltransferase families (FUT10 and FUT11). J Biol Chem 284:4723–4738PubMedCrossRefGoogle Scholar
  19. Moriwaki K, Miyoshi E (2010) Fucosylation and gastrointestinal cancer. World J Hepatol 2:151–161PubMedCentralPubMedCrossRefGoogle Scholar
  20. Oriol R, Opelz G, Chun C, Terasaki PI (1980) The Lewis system and kidney transplantation. Transplantation 29:397–400PubMedCrossRefGoogle Scholar
  21. Paschinger K, Rendic D, Lochnit G, Jantsch V, Wilson IB (2004) Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans. J Biol Chem 279:49588–49598PubMedCrossRefGoogle Scholar
  22. Paschinger K, Rendic D, Wilson IB (2009) Revealing the anti-HRP epitope in Drosophila and Caenorhabditis. Glycoconjugate J 26:385–395CrossRefGoogle Scholar
  23. Patnaik SK (2007) Characterization of Fut10 and Fut11, putative α1-3/4 fucosyltransferase genes important for vertebrate development. Nat Proc.
  24. Reinke SO, Bayer M, Berger M, Hinderlich S, Blanchard V (2012) The analysis of N-glycans of cell membrane proteins from human hematopoietic cell lines reveals distinctions in their pattern. Biol Chem 393:731–747PubMedCrossRefGoogle Scholar
  25. Rendic D, Linder A, Paschinger K, Borth N, Wilson IBH, Fabini G (2006) Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells. J Biol Chem 281:3343–3353PubMedCrossRefGoogle Scholar
  26. Rendic D, Klaudiny J, Stemmer U, Schmidt J, Paschinger K, Wilson IB (2007) Towards abolition of immunogenic structures in insect cells: characterization of a honey-bee (Apis mellifera) multi-gene family reveals both an allergy-related core α1,3-fucosyltransferase and the first insect Lewis-histo-blood-group-related antigen-synthesizing enzyme. Biochem J 402:105–115PubMedCrossRefGoogle Scholar
  27. Roos C, Kolmer M, Mattila P, Renkonen R (2002) Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. J Biol Chem 277:3168–3175PubMedCrossRefGoogle Scholar
  28. Stahl M, Uemura K, Ge C, Shi S, Tashima Y, Stanley P (2008) Roles of Pofut1 and O-fucose in mammalian notch signaling. J Biol Chem 283:13638–13651PubMedCrossRefGoogle Scholar
  29. Sun HY, Lin SW, Ko TP, Pan JF, Liu CL, Lin CN, Wang AH, Lin CH (2007) Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design. J Biol Chem 282:9973–9982PubMedCrossRefGoogle Scholar
  30. Tretter V, Altmann F, Kubelka V, März L, Becker WM (1993) Fucose α1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. Int Arch Allergy Immunol 102:259–266PubMedCrossRefGoogle Scholar
  31. van Die I, Gomord V, Kooyman FN, van den Berg TK, Cummings RD, Vervelde L (1999) Core α1,3-fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep. FEBS Lett 463:189–193PubMedCrossRefGoogle Scholar
  32. Weston BW, Nair RP, Larsen RD, Lowe JB (1992) Isolation of a novel human α(1,3)-fucosyltransferase gene and molecular comparison to the human Lewis blood group α(1,3/1,4)-fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. J Biol Chem 267:4152–4160PubMedGoogle Scholar
  33. Wilson IB, Harthill JE, Mullin NP, Ashford DA, Altmann F (1998) Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts. Glycobiology 8:651–661PubMedCrossRefGoogle Scholar

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© Springer Japan 2014

Authors and Affiliations

  1. 1.Reponses cellulaires au microenvironement et cancerCNRS and INSERM U1004VillejuifFrance
  2. 2.Inserm U1004 Reponses cellulaires au microenvironement et cancerCNRS et L’Université de Paris Sud XIVillejuifFrance

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