ArticleThe Biochemical journal2015
Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026Review
- Targeting the Endoplasmic Reticulum Oxidoreductin-1 Alpha-Protein Disulfide Isomerase Redox Interface as a Therapeutic Strategy in Cancer.Biomedicines · 2026Review
- Transmembrane thiol isomerase TMX1 counterbalances the effect of ERp46 to inhibit platelet activation and integrin αIIbβ3 function.Research and practice in thrombosis and haemostasis · 2024Article
- Recent advances in vascular thiol isomerases and redox systems in platelet function and thrombosis.Journal of thrombosis and haemostasis : JTH · 2024Review
- Protein disulfide isomerase cleaves allosteric disulfides in histidine-rich glycoprotein to regulate thrombosis.Nature communications · 2024Article
- Thioredoxin Domain Containing 5 (TXNDC5): Friend or Foe?Current issues in molecular biology · 2024Review
- Distinct role of ERp57 and ERdj5 as a disulfide isomerase and reductase during ER protein folding.Journal of cell science · 2023Article
- Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging.Structure (London, England : 1993) · 2022Article
- Pathways Linking Nicotinamide Adenine Dinucleotide Phosphate Production to Endoplasmic Reticulum Protein Oxidation and Stress.Frontiers in molecular biosciences · 2022Review
- Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis.Antioxidants & redox signaling · 2021Review
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Vascular thiol isomerases in thrombosis: The yin and yang.Journal of thrombosis and haemostasis : JTH · 2020Review
- Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway.Cells · 2020Review
- Ciclopirox activates PERK-dependent endoplasmic reticulum stress to drive cell death in colorectal cancer.Cell death & disease · 2020Article
- Pathological consequences of the unfolded protein response and downstream protein disulphide isomerases in pulmonary viral infection and disease.Journal of biochemistry · 2020Review
- Regulation of plant ER oxidoreductin 1 (ERO1) activity for efficient oxidative protein folding.The Journal of biological chemistry · 2019Article
- Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.The Journal of biological chemistry · 2019Review
- Identification of the physiological substrates of PDIp, a pancreas-specific protein-disulfide isomerase family member.The Journal of biological chemistry · 2018Article
- Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation.The Journal of biological chemistry · 2018Article
- Lipase maturation factor 1 affects redox homeostasis in the endoplasmic reticulum.The EMBO journal · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The formation of disulfides in proteins entering the secretory pathway is catalysed by the protein disulfide isomerase (PDI) family of enzymes. These enzymes catalyse the introduction, reduction and isomerization of disulfides. To function continuously they require an oxidase to reform the disulfide at their active site. To determine how each family member can be recycled to catalyse disulfide exchange, we have studied whether disulfides are transferred between individual PDI family members. We studied disulfide exchange either between purified proteins or by identifying mixed disulfide formation within cells grown in culture. We show that disulfide exchange occurs efficiently and reversibly between specific PDIs. These results have allowed us to define a hierarchy for members of the PDI family, in terms of ability to act as electron acceptors or donors during thiol-disulfide exchange reactions and indicate that there is no kinetic barrier to the exchange of disulfides between several PDI proteins. Such promiscuous disulfide exchange negates the necessity for each enzyme to be oxidized by Ero1 (ER oxidoreductin 1) or reduced by a reductive system. The lack of kinetic separation of the oxidative and reductive pathways in mammalian cells contrasts sharply with the equivalent systems for native disulfide formation within the bacterial periplasm.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.