Glycosylation-directed quality control of protein folding

Nat Rev Mol Cell Biol. 2015 Dec;16(12):742-52. doi: 10.1038/nrm4073. Epub 2015 Oct 14.

Abstract

Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated in the endoplasmic reticulum. These adducts have many biological functions, including, notably, their contribution to the maturation of glycoproteins. N-linked glycans are of oligomeric structure, forming configurations that provide blueprints to precisely instruct the folding of protein substrates and the quality control systems that scrutinize it. O-linked mannoses are simpler in structure and were recently found to have distinct functions in protein quality control that do not require the complex structure of N-linked glycans. Together, recent studies reveal the breadth and sophistication of the roles of these glycan-directed modifications in protein biogenesis.

Publication types

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

MeSH terms

  • Animals
  • Endoplasmic Reticulum / metabolism*
  • Glycoproteins / chemistry*
  • Glycosylation
  • Humans
  • Polysaccharides / chemistry*
  • Protein Folding*
  • Protein Processing, Post-Translational*
  • Protein Structure, Tertiary
  • Schizosaccharomyces / metabolism

Substances

  • Glycoproteins
  • Polysaccharides