Non-lysosomal degradation pathway for N-linked glycans and dolichol-linked oligosaccharides

Biochem Biophys Res Commun. 2014 Oct 17;453(2):213-9. doi: 10.1016/j.bbrc.2014.05.075. Epub 2014 May 24.

Abstract

There is growing evidence that asparagine (N)-linked glycans play pivotal roles in protein folding and intra- or intercellular trafficking of N-glycosylated proteins. During the N-glycosylation of proteins, significant amounts of free oligosaccharides (fOSs) and phosphorylated oligosaccharides (POSs) are generated at the endoplasmic reticulum (ER) membrane by unclarified mechanisms. fOSs are also formed in the cytosol by the enzymatic deglycosylation of misfolded glycoproteins destined for proteasomal degradation. This article summarizes the current knowledge of the molecular and regulatory mechanisms underlying the formation of fOSs and POSs in mammalian cells and Saccharomyces cerevisiae.

Keywords: Free oligosaccharides; Non-lysosomal degradation; Oligosaccharyltransferase; Peptide:N-glycanase; Phosphorylated oligosaccharides; Pyrophosphatase.

Publication types

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

MeSH terms

  • Animals
  • Biological Transport, Active
  • Cytosol / metabolism
  • Dolichols / metabolism*
  • Endoplasmic Reticulum / metabolism
  • Glycosylation
  • Humans
  • Models, Biological
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism*
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Folding
  • Pyrophosphatases / metabolism

Substances

  • Dolichols
  • Oligosaccharides
  • Polysaccharides
  • Pyrophosphatases