Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors

Curr Opin Struct Biol. 2011 Oct;21(5):583-9. doi: 10.1016/j.sbi.2011.08.008. Epub 2011 Sep 15.

Abstract

The Notch family of receptors plays essential roles in many phases of development, and dysregulation of Notch activity is increasingly recognized as a player in many diseases. O-Glycosylation of the Notch extracellular domain is essential for Notch activity, and tissue-specific alterations in the glycan structures are known to regulate activity. Here we review recent advances in identification and characterization of the enzymes responsible for glycosylating Notch and molecular mechanisms for how these O-glycans affect Notch activity.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Drosophila / metabolism
  • Drosophila Proteins / metabolism*
  • Fucose / metabolism
  • Fucosyltransferases / metabolism
  • Glucose / metabolism
  • Glucosyltransferases / metabolism
  • Glycosylation
  • Mammals
  • Mice
  • N-Acetylglucosaminyltransferases / metabolism*
  • Polysaccharides / metabolism*
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Notch / metabolism*
  • Signal Transduction
  • Structure-Activity Relationship

Substances

  • Drosophila Proteins
  • N protein, Drosophila
  • Polysaccharides
  • Receptors, Notch
  • Fucose
  • Fucosyltransferases
  • Glucosyltransferases
  • N-Acetylglucosaminyltransferases
  • Rumi protein, Drosophila
  • Pofut1 protein, mouse
  • fng protein, Drosophila
  • Glucose