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

Anna Fassio, Roberto Sitia

Research output: Contribution to journalArticlepeer-review

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

Keywords

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

ASJC Scopus subject areas

  • Cell Biology
  • Instrumentation

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