Versatility of the endoplasmic reticulum protein folding factory

Crit Rev Biochem Mol Biol. Jul-Aug 2005;40(4):191-228. doi: 10.1080/10409230591008161.

Abstract

The endoplasmic reticulum (ER) is dedicated to import, folding and assembly of all proteins that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is special. For instance, newly synthesized proteins are N-glycosylated and by default form disulfide bonds in the ER, but not elsewhere in the cell. In this review, we discuss which features distinguish the ER as an efficient folding factory, how the ER monitors its output and how it disposes of folding failures.

Publication types

  • Review

MeSH terms

  • Endoplasmic Reticulum / metabolism*
  • Glycoproteins / metabolism
  • Glycosylation
  • Hydrophobic and Hydrophilic Interactions
  • Models, Biological
  • Molecular Chaperones / biosynthesis
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Protein Denaturation
  • Protein Folding*
  • Quality Control
  • Signal Transduction / physiology
  • Ubiquitin / metabolism

Substances

  • Glycoproteins
  • Molecular Chaperones
  • Ubiquitin