Protein Folding in the Endoplasmic Reticulum
Protein Folding in the Endoplasmic Reticulum
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DOI：
10.1101/cshperspect.a013201
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发表时间：
2013-05-01
影响因子：
7.2
通讯作者：
Hebert, Daniel N.
中科院分区：
文献类型：
--
作者：
Braakman, Ineke;Hebert, Daniel N.
在本文中，我们将探讨内质网（ER）腔中蛋白质的折叠，包括三种共价修饰的作用：信号肽切除、N - 连接糖基化和二硫键形成，以及内质网驻留折叠因子的功能和重要性。这些折叠因子包括经典的分子伴侣及其辅分子伴侣、糖类结合分子伴侣，以及蛋白质二硫键异构酶（PDI）和脯氨酸顺反异构酶家族的折叠催化剂。最后我们将从折叠蛋白质的角度进行总结：对作为内质网机制的“客户”而在内质网中转运的蛋白质的特性、折叠和输出速率进行比较。
In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline cis-trans isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.