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Related Experiment Videos

Pathways for protein disulphide bond formation.

A R Frand1, J W Cuozzo, C A Kaiser

  • 1Dept of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.

Trends in Cell Biology
|April 8, 2000
PubMed
Summary
This summary is machine-generated.

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Disulphide bond formation in the endoplasmic reticulum (ER) is crucial for secretory protein folding. New findings reveal glutathione oxidation competes with protein thiol oxidation in this pathway.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Genetics

Background:

  • Secretory protein folding relies on disulphide bond formation.
  • The endoplasmic reticulum (ER) hosts a core pathway for these bonds.
  • Eukaryotic disulphide bond formation involves Ero1p and protein disulphide isomerase (PDI).

Purpose of the Study:

  • To outline the core pathway for disulphide bond formation in the ER.
  • To investigate the role of Ero1p and PDI in oxidative folding.
  • To explore the competition between glutathione and protein thiol oxidation.

Main Methods:

  • Review of recent advances in genetics and cell biology.
  • Analysis of the ER pathway for disulphide bond formation.
  • Discussion of PDI homologues and prokaryotic systems.

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Main Results:

  • Oxidizing equivalents flow from Ero1p to secretory proteins via PDI.
  • Glutathione oxidation in the ER competes with protein thiol oxidation, contrary to expectations.
  • Contributions of PDI homologues to oxidative folding catalysis.

Conclusions:

  • The ER pathway for disulphide bond formation is increasingly understood.
  • Glutathione's role in ER redox balance is complex and competitive.
  • Similarities exist between eukaryotic and prokaryotic disulphide-bond-forming systems.