Pathways for protein disulphide bond formation

The folding of many secretory proteins depends upon the formation of disulphide bonds. Recent advances in genetics and cell biology have outlined a core pathway for disulphide bond formation in the endoplasmic reticulum (ER) of eukaryotic cells. In this pathway, oxidizing equivalents flow from the r...

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Bibliographic Details
Published inTrends in cell biology Vol. 10; no. 5; pp. 203 - 210
Main Authors Frand, A R, Cuozzo, J W, Kaiser, C A
Format Journal Article
LanguageEnglish
Published England 01.05.2000
Subjects
Animals
Cysteine - metabolism
Disulfides - chemistry
Disulfides - metabolism
Endoplasmic Reticulum - chemistry
Endoplasmic Reticulum - metabolism
Glycoproteins - metabolism
Humans
Membrane Glycoproteins
Oxidation-Reduction
Oxidoreductases
Protein Disulfide-Isomerases - metabolism
Protein Folding
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Summary:The folding of many secretory proteins depends upon the formation of disulphide bonds. Recent advances in genetics and cell biology have outlined a core pathway for disulphide bond formation in the endoplasmic reticulum (ER) of eukaryotic cells. In this pathway, oxidizing equivalents flow from the recently identified ER membrane protein Ero1p to secretory proteins via protein disulphide isomerase (PDI). Contrary to prior expectations, oxidation of glutathione in the ER competes with oxidation of protein thiols. Contributions of PDI homologues to the catalysis of oxidative folding will be discussed, as will similarities between eukaryotic and prokaryotic disulphide-bond-forming systems.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ObjectType-Review-1
ISSN:0962-8924
DOI:10.1016/s0962-8924(00)01745-1