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

Anna Fassio, Roberto Sitia

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)151-157
Number of pages7
JournalHistochemistry and Cell Biology
Volume117
Issue number2
DOIs
Publication statusPublished - 2002

Fingerprint

endoplasmic reticulum
disulfides
Isomerization
quality control
Endoplasmic Reticulum
Disulfides
Quality Control
isomerization
Quality control
proteins
Proteins
folding
Protein folding
Protein Folding
Yeast
Oxidation-Reduction
yeast
Yeasts
Cells
Molecules

Keywords

  • Degradation
  • Endoplasmic reticulum
  • Membrane insertion
  • Oxidative protein folding
  • Redox

ASJC Scopus subject areas

  • Cell Biology
  • Instrumentation

Cite this

@article{a5092579e540461790b51c555039f732,
title = "Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum",
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.",
keywords = "Degradation, Endoplasmic reticulum, Membrane insertion, Oxidative protein folding, Redox",
author = "Anna Fassio and Roberto Sitia",
year = "2002",
doi = "10.1007/s00418-001-0364-0",
language = "English",
volume = "117",
pages = "151--157",
journal = "Histochemistry and Cell Biology",
issn = "0948-6143",
publisher = "Springer Verlag",
number = "2",

}

TY - JOUR

T1 - Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum

AU - Fassio, Anna

AU - Sitia, Roberto

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - Degradation

KW - Endoplasmic reticulum

KW - Membrane insertion

KW - Oxidative protein folding

KW - Redox

UR - http://www.scopus.com/inward/record.url?scp=0036186384&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036186384&partnerID=8YFLogxK

U2 - 10.1007/s00418-001-0364-0

DO - 10.1007/s00418-001-0364-0

M3 - Article

C2 - 11935291

AN - SCOPUS:0036186384

VL - 117

SP - 151

EP - 157

JO - Histochemistry and Cell Biology

JF - Histochemistry and Cell Biology

SN - 0948-6143

IS - 2

ER -