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Glycosyltransferases Involved in O-fucose Glycan Synthesis

  • Tetsuya Okajima
  • Tsukasa Matsuda

Abstract

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).

Keywords

Epidermal Growth Factor Sialic Acid Notch Signaling Notch Signaling Pathway Notch Receptor 
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.

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References

  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
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Copyright information

© 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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