A method to the madness of N-glycan complexity?

Cell. 2007 Apr 6;129(1):27-9. doi: 10.1016/j.cell.2007.03.022.

Abstract

Cell-surface glycoprotein receptors have varying numbers of N-glycan sites. In this issue of Cell, Lau et al. (2007) report that increasing intracellular UDP-GlcNAc leads to increased branching of N-glycans, increased receptor association with cell-surface galectin-3, and enhanced signaling. They also show that the kinetics of this response differ between growth-promoting receptors, which have 8-16 N-glycans, and those that induce growth arrest, which have very few N-glycans, suggesting that hexosamine flux may regulate the transition from growth to arrest.

Publication types

  • Comment

MeSH terms

  • Animals
  • Galectin 3 / metabolism
  • Glycosylation
  • Hexosamines / metabolism
  • Mice
  • N-Acetylglucosaminyltransferases / metabolism
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Uridine Diphosphate N-Acetylglucosamine / metabolism

Substances

  • Galectin 3
  • Hexosamines
  • Polysaccharides
  • Uridine Diphosphate N-Acetylglucosamine
  • N-Acetylglucosaminyltransferases