Institute of Molecular, Cell and Systems Biology, College of Medical Veterinary and Life Sciences, Davidson Building, University of Glasgow, Glasgow G12 8QQ, UK.
Cells. 2020 Aug 29;9(9):1994. doi: 10.3390/cells9091994.
Disulphide 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 disulphide bond formation is the endoplasmic reticulum (ER). How cysteines correctly pair during polypeptide folding to form the native disulphide bond pattern is a complex problem that is not fully understood. In this paper, the evidence for different folding mechanisms involved in ER-localised disulphide bond formation is reviewed with emphasis on events that occur during ER entry. Disulphide 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 disulphide isomerase (PDI) family members. This review highlights the complex array of cellular processes that influence disulphide bond formation and identifies key questions that need to be addressed to further understand this fundamental process.
二硫键是所有生命领域中蛋白质的丰富特征，对结构、稳定性和功能很重要。在真核细胞中，二硫键形成的主要部位是内质网（ER）。半胱氨酸在多肽折叠过程中如何正确配对形成天然二硫键模式是一个复杂的问题，目前尚未完全了解。本文综述了 ER 定位中二硫键形成所涉及的不同折叠机制的证据，重点是 ER 进入时发生的事件。讨论了新生多肽中二硫键的形成，重点关注：（i）其与构象折叠的机制关系，（ii）在 ER 进入的共翻译阶段发生的证据，以及（iii）蛋白二硫键异构酶（PDI）家族成员的作用。本综述强调了影响二硫键形成的一系列复杂细胞过程，并确定了需要解决的关键问题，以进一步了解这一基本过程。
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