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Journal of Zhejiang University SCIENCE B 2024 Vol.25 No.3 P.212-232

http://doi.org/10.1631/jzus.B2300403


Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells


Author(s):  Hong CAO, Xuchang ZHOU, Bowen XU, Han HU, Jianming GUO, Yuwei MA, Miao WANG, Nan LI, Jun ZOU

Affiliation(s):  Department of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China; more

Corresponding email(s):   junzou@sus.edu.cn, linan@immunol.org

Key Words:  Endoplasmic reticulum-associated degradation (ERAD), Protein folding, Ubiquitination, Retrotranslocation


Hong CAO, Xuchang ZHOU, Bowen XU, Han HU, Jianming GUO, Yuwei MA, Miao WANG, Nan LI, Jun ZOU. Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells[J]. Journal of Zhejiang University Science B, 2024, 25(3): 212-232.

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author="Hong CAO, Xuchang ZHOU, Bowen XU, Han HU, Jianming GUO, Yuwei MA, Miao WANG, Nan LI, Jun ZOU",
journal="Journal of Zhejiang University Science B",
volume="25",
number="3",
pages="212-232",
year="2024",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B2300403"
}

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%A Hong CAO
%A Xuchang ZHOU
%A Bowen XU
%A Han HU
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%A Yuwei MA
%A Miao WANG
%A Nan LI
%A Jun ZOU
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%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B2300403

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A1 - Hong CAO
A1 - Xuchang ZHOU
A1 - Bowen XU
A1 - Han HU
A1 - Jianming GUO
A1 - Yuwei MA
A1 - Miao WANG
A1 - Nan LI
A1 - Jun ZOU
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VL - 25
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SP - 212
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PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B2300403


Abstract: 
The endoplasmic reticulum is a key site for protein production and quality control. More than one-third of proteins are synthesized and folded into the correct three-dimensional conformation in the endoplasmic reticulum. However, during protein folding, unfolded and/or misfolded proteins are prone to occur, which may lead to endoplasmic reticulum stress. Organisms can monitor the quality of the proteins produced by endoplasmic reticulum quality control (ERQC) and endoplasmic reticulum-associated degradation (ERAD), which maintain endoplasmic reticulum protein homeostasis by degrading abnormally folded proteins. The underlying mechanisms of protein folding and ERAD in mammals have not yet been fully explored. Therefore, this paper reviews the process and function of protein folding and ERAD in mammalian cells, in order to help clinicians better understand the mechanism of ERAD and to provide a scientific reference for the treatment of diseases caused by abnormal ERAD.

哺乳动物细胞蛋白质折叠和内质网相关降解的研究进展

曹红1, 2,周绪昌1,徐博文2,胡涵2,郭健民1,马誉玮1,王淼1,李楠2,邹军1
1上海体育大学运动健康学院,中国上海市,200438
2海军军医大学,免疫与炎症全国重点实验室,中国上海市,200433
摘要:内质网是体内蛋白质产生和质量控制的关键场所,体内约1/3的蛋白是经内质网合成并加工发挥作用。蛋白质合成后需要进行一定的折叠,形成正确的三维构象,从而发挥其功能。然而在蛋白质折叠过程中易出现错误,导致未折叠和(或)错误折叠蛋白在内质网内聚集,进而导致内质网应激。对此,机体可通过内质网质量控制(ERQC)和内质网相关降解(ERAD)对生成的蛋白质质量进行检测,并通过降解异常折叠蛋白质,以维持内质网内蛋白稳态。目前为止,对哺乳动物体内有关蛋白质折叠和ERAD的详细机制描述尚不全面。为此,本文综述了哺乳动物细胞中蛋白质折叠与ERAD的过程和功能,并重点对ERAD相关蛋白质构象疾病的潜在病理生理学进行了介绍。

关键词:内质网相关降解;蛋白质折叠;泛素化;逆向转位

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

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