Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation
By Feras Hatahet, L. Ruddock. Antioxidants and Redox Signaling, 2009
657 citations recorded by the source corpus.
Disulfide bond formation is probably involved in the biogenesis of approximately one third of human proteins. A central player in this essential process is protein disulfide isomerase or PDI. PDI was the first protein-folding catalyst reported. However, despite more than four decades of study, we still do not understand much about its physiological mechanisms of action. This review examines the published literature with a critical eye. This review aims to (a) provide background on the chemistry of disulfide bond formation and rearrangement, including the concept of reduction potential, before examining the structure of PDI; (b) detail the thiol-disulfide exchange reactions that are catalyzed by PDI in vitro, including a critical examination of the assays used to determine them; (c) examine oxidation and reduction of PDI in vivo, including not only the role of ERo1 but also an extensive assessment of the role of glutathione, as well as other systems, such as peroxide, dehydroascorbate, and a discussion of vitamin K–based systems; (d) consider the in vivo reactions of PDI and the determination and implications of the redox state of PDI in vivo; and (e) discuss other human and yeast PDI-family members. Antioxid. Redox Signal. 11, 2807–2850.
Subfields: Cell Biology, Insect Science, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e1f53ab21c48d2c7aec519d604e925d8522ebc9d
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Citations in the corpus
- Antioxidant responses and cellular adjustments to oxidative stress (2015, background): “Within that system, the ER resident oxidoreductase Ero1 and protein disulfide isomerase (PDI) appear to play key roles [134,135].”
- Probing the Mutational Interplay between Primary and Promiscuous Protein Functions: A Computational-Experimental Approach (2012, background): “(see Figure 3), involves a nucleophilic attack of the substrate on the disulfide bridge of the oxidized enzyme and the mixed-disulfide intermediate is resolved by attack from the free cysteine (in the thiolate form) of the substrate [36].”
- Multiple catalytically active thioredoxin folds: a winning strategy for many functions (2010, background): “For this purpose, the cell produces a large number of proteins, belonging to the protein disulfide isomerase (PDI) family, which catalyze the oxidation and isomerization of disulfide bonds [7, 28].”
- Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli (2011, background): “The formation of native disulfide bonds is often the rate limiting step of protein biogenesis [1-3].”
- Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli (2010, background): “While the redox potential of the ER is more oxidizing than that of the cytoplasm it is still a compartment in which disulfide bond reduction and isomerization must occur [1] i.”