Glycosyltransferases Involved in O-fucose Glycan Synthesis

  • Tetsuya Okajima
  • Tsukasa Matsuda


Modification with O-fucose glycans is a rare type of post-translational modification found mainly on epidermal growth factor (EGF) domains. Although EGF domains are generally found on a number of secreted or cell surface glycoproteins, only a subset can be O-fucosylated. Founding members of those O-fucosylated proteins include urokinase in human urine and the coagulation/fibrinolytic proteins in blood plasma, such as blood clotting Factors VII, IX, and XII, and tissue plasminogen activator. Recently, a number of transmembrane proteins involved in the Notch signaling pathway have been identified as novel O-fucosylated glycoproteins. The extracellular domain of the Notch receptor is composed largely of a tandem array of EGF repeats (36 in Drosophila Notch and mammalian Notch1 and Notch2) and many of them are considered to be O-fucosylated. Similarly, Notch ligands (Delta, Serrate/Jagged) as well as Dlk-1/Pref-1, a negative regulator for Notch signaling, are also EGF repeat-containing proteins that are known to be O-fucosylated. By comparing the sequences surrounding the sites of O-fucose modification of those glycoproteins, the consensus amino acid sequence for O-fucosylation is proposed to be C2X3–5 S/TC3 (where C2 and C3 are the second and third conserved cysteine residue, respectively, X3–5 are any 3–5 amino acids, and S/T is the fucosylated amino acid) (Haltiwanger and Stanley 2002).


Epidermal Growth Factor Sialic Acid Notch Signaling Notch Signaling Pathway Notch Receptor 
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  1. Haines N, Irvine KD (2003) Glycosylation regulates Notch signalling. Nat Rev Mol Cell Biol 4:786–797PubMedGoogle Scholar
  2. Haltiwanger RS, Stanley P (2002) Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase. Biochim Biophys Acta 1573:328–335PubMedGoogle Scholar
  3. Moloney DJ, Panin VM, Johnston SH, Chen J, Shao L, Wilson R, Wang Y, Stanley P, Irvine KD, Haltiwanger RS, Vogt TF (2000) Fringe is a glycosyltransferase that modifies Notch. Nature 406:369–375PubMedCrossRefGoogle Scholar
  4. Okajima T, Irvine KD (2002) Regulation of Notch signaling by O-linked fucose. Cell 111:893–904PubMedCrossRefGoogle Scholar
  5. Okajima T, Xu A, Irvine KD (2003) Modulation of Notch-ligand binding by protein O-fucosyltransferase 1 and fringe. J Biol Chem 278:42340–42345PubMedCrossRefGoogle Scholar

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© Springer 2008

Authors and Affiliations

  • Tetsuya Okajima
    • 1
  • Tsukasa Matsuda
    • 1
  1. 1.Department of Applied Molecular BiosciencesNagoya University Graduate School of Bioagricultural SciencesNagoyaJapan

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