Robinson, P. J. and Bulleid, N. J. (2020) Mechanisms of disulfide bond formation in nascent polypeptides entering the secretory pathway. Cells, 9(9), 1994. (doi: 10.3390/cells9091994) (PMID:32872499)
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Abstract
Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER). How cysteines correctly pair during polypeptide folding to form the native disulfide bond pattern is a complex problem that is not fully understood. In this paper, the evidence for different folding mechanisms involved in ER-localised disulfide bond formation is reviewed with emphasis on events that occur during ER entry. Disulfide formation in nascent polypeptides is discussed with focus on (i) its mechanistic relationship with conformational folding, (ii) evidence for its occurrence at the co-translational stage during ER entry, and (iii) the role of protein disulfide isomerase (PDI) family members. This review highlights the complex array of cellular processes that influence disulfide bond formation and identifies key questions that need to be addressed to further understand this fundamental process.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Bulleid, Professor Neil and Robinson, Dr Philip |
| Authors: | Robinson, P. J., and Bulleid, N. J. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
| Journal Name: | Cells |
| Publisher: | MDPI |
| ISSN: | 2073-4409 |
| ISSN (Online): | 2073-4409 |
| Published Online: | 29 August 2020 |
| Copyright Holders: | Copyright © 2020 The Authors |
| First Published: | First published in Cells 9(9): 1994 |
| Publisher Policy: | Reproduced under a Creative Commons License |
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