Protein folding in the endoplasmic reticulum

Cold Spring Harb Perspect Biol. 2013 May 1;5(5):a013201. doi: 10.1101/cshperspect.a013201.

Abstract

In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline cis-trans isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.

Publication types

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

MeSH terms

  • Endoplasmic Reticulum / metabolism*
  • Glycosylation
  • Models, Biological
  • Molecular Chaperones / metabolism
  • Molecular Chaperones / physiology
  • Protein Folding*
  • Protein Modification, Translational
  • Protein Processing, Post-Translational

Substances

  • Molecular Chaperones