Histochemistry and Cell Biology

, Volume 117, Issue 2, pp 151–157

Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum

  • Anna Fassio
  • Roberto Sitia
Review

DOI: 10.1007/s00418-001-0364-0

Cite this article as:
Fassio, A. & Sitia, R. Histochem Cell Biol (2002) 117: 151. doi:10.1007/s00418-001-0364-0

Abstract.

Efficient protein folding and quality control in the endoplasmic reticulum (ER) require that disulphide bonds are formed in nascent proteins, isomerised during assisted folding and reduced in terminally misfolded molecules. Recent findings in yeast and mammalian cells indicate that specific protein–protein interactions underlie redox control in the ER, allowing these competing reactions to occur simultaneously during protein quality control.

Degradation Endoplasmic reticulum Membrane insertion Oxidative protein folding Redox

Copyright information

© Springer-Verlag 2002

Authors and Affiliations

  • Anna Fassio
    • 1
  • Roberto Sitia
    • 1
  1. 1.DiBiT-HSR and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milan, ItalyItaly
  2. 2.Present address: Department of Experimental Medicine, Section of Physiology, University of Genoa, ItalyItaly