ArticleThe Journal of biological chemistry2016
Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Transcriptomics analysis identifies folding and secretion related genes for improving monoclonal antibody production in Thermothelomyces heterothallica C1.Microbial cell factories · 2026Article
- ERO1-PDI Redox Signaling in Health and Disease.Antioxidants & redox signaling · 2021Review
- Mutual interaction between endoplasmic reticulum and mitochondria in nonalcoholic fatty liver disease.Lipids in health and disease · 2020Review
- Regulation of plant ER oxidoreductin 1 (ERO1) activity for efficient oxidative protein folding.The Journal of biological chemistry · 2019Article
- Quantitative Analyses of the Yeast Oxidative Protein Folding PathwayAntioxidants & redox signaling · 2019Article
- Prompting Fab Yeast Surface Display Efficiency by ER Retention and Molecular Chaperon Co-expression.Frontiers in bioengineering and biotechnology · 2019Article
- Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α.The EMBO journal · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Cysteine residues in a yeast viral A/B toxin crucially control host cell killing via pH-triggered disulfide rearrangements.Molecular biology of the cell · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of disulfide bonds in the endoplasmic reticulum (ER) of eukaryotic cells is catalyzed by the sulfhydryl oxidase, ER oxidoreductin 1 (Ero1), and protein-disulfide isomerase (PDI). PDI is oxidized by Ero1 to continuously introduce disulfides into substrates, and feedback regulates Ero1 activity by manipulating the regulatory disulfides of Ero1. In this study we find that yeast Ero1p is enzymatically active even with its regulatory disulfides intact, and further activation of Ero1p by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in Pdi1p. The principal client-binding site in the Pdi1pb' domain is necessary not only for the functional Ero1p-Pdi1p disulfide relay but also for the activation of Ero1p. We also demonstrate by complementary activation assays that the regulatory disulfides in Ero1p are much more stable than those in human Ero1α. These new findings on yeast Ero1p-Pdi1p interplay reveal significant differences from our previously identified mode of human Ero1α-PDI interplay and provide insights into the evolution of the eukaryotic oxidative protein folding pathway.
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