Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway
Abstract
:1. Introduction
2. Mechanisms of Disulfide Bond Formation during Protein Folding
3. Disulfide Bond Formation in Nascent Polypeptides during Translocation
3.1. The Folding of Proteins at the Co-Translational Stage
3.2. Capturing Disulfide Bond Formation during Folding in Cells
3.3. Evidence for Disulfide Bond Formation in Translation Intermediates
4. The Role of PDI Family Members in Nascent Polypeptide Folding
4.1. The PDI Family Acts via the Mechanism of Thiol–Disulfide Exchange
4.2. Oxidation Pathways to Re-Activate PDI Family Members Following Catalysis of Disulfide Bond Formation
4.3. PDI Preferentially Interacts with Unfolded Substrates to Catalyse Disulfide Bond Formation
4.4. Evidence for Disulfide Reduction and Rearrangements at the Co-Translational Stage
5. Conclusions and Future Directions
5.1. What Are the Structures of Translation Intermediates and How Do They Change throughout Translocation?
5.2. How Does Our Understanding of Co-Translational Folding and Disulfide Bond Formation Apply across the Proteome?
5.3. How and When Do Folding Factors Interact with Nascent Polypeptides?
Author Contributions
Funding
Conflicts of Interest
References
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Robinson, P.J.; Bulleid, N.J. Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway. Cells 2020, 9, 1994. https://doi.org/10.3390/cells9091994
Robinson PJ, Bulleid NJ. Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway. Cells. 2020; 9(9):1994. https://doi.org/10.3390/cells9091994
Chicago/Turabian StyleRobinson, Philip J., and Neil J. Bulleid. 2020. "Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway" Cells 9, no. 9: 1994. https://doi.org/10.3390/cells9091994