Glycosylation regulates Notch signalling

Nat Rev Mol Cell Biol. 2003 Oct;4(10):786-97. doi: 10.1038/nrm1228.

Abstract

Intracellular post-translational modifications such as phosphorylation and ubiquitylation have been well studied for their roles in regulating diverse signalling pathways, but we are only just beginning to understand how differential glycosylation is used to regulate intercellular signalling. Recent studies make clear that extracellular post-translational modifications, in the form of glycosylation, are essential for the Notch signalling pathway, and that differences in the extent of glycosylation are a significant mechanism by which this pathway is regulated.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Biological Clocks
  • Body Patterning
  • Drosophila Proteins
  • Epidermal Growth Factor / metabolism
  • Fucose / chemistry
  • Fucose / metabolism
  • Fucosyltransferases / metabolism
  • Glycosylation
  • Membrane Proteins / metabolism*
  • N-Acetylglucosaminyltransferases / metabolism
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism
  • Protein Processing, Post-Translational
  • Receptors, Notch
  • Signal Transduction / physiology*
  • Wings, Animal / physiology

Substances

  • Drosophila Proteins
  • Membrane Proteins
  • Polysaccharides
  • Receptors, Notch
  • Fucose
  • Epidermal Growth Factor
  • Fucosyltransferases
  • N-Acetylglucosaminyltransferases
  • fng protein, Drosophila