School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan.
Int J Mol Sci. 2020 Dec 8;21(24):9351. doi: 10.3390/ijms21249351.
Complicated and sophisticated protein homeostasis (proteostasis) networks in the endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their regulators, help to maintain cell viability. Newly synthesized proteins inserted into the ER need to fold and assemble into unique native structures to fulfill their physiological functions, and this is assisted by protein disulfide isomerase (PDI) family. Herein, we focus on recent advances in understanding the detailed mechanisms of PDI family members as guides for client folding and assembly to ensure the efficient production of secretory proteins.
内质网（ER）中复杂而精细的蛋白质动态平衡（proteostasis）网络，包括二硫键催化剂、分子伴侣及其调节剂，有助于维持细胞活力。新合成的蛋白质需要插入 ER 中折叠并组装成独特的天然结构以发挥其生理功能，这得到了蛋白质二硫键异构酶（PDI）家族的帮助。在此，我们重点介绍了近年来对 PDI 家族成员作为指导客户折叠和组装的详细机制的理解的最新进展，以确保分泌蛋白的有效生产。
