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

作　　者：Hong CAO Xuchang ZHOU Bowen XU Han HU Jianming GUO Yuwei MA Miao WANG Nan LI Jun ZOU 

机构地区：[1]Department of Sport Rehabilitation,Shanghai University of Sport,Shanghai 200438,China [2]National Key Laboratory of Immunity and Inflammation,Naval Medical University,Shanghai 200433,China

出　　处：《Journal of Zhejiang University-Science B(Biomedicine & Biotechnology)》2024年第3期212-232,共21页浙江大学学报（英文版）B辑（生物医学与生物技术）

基　　金：This work was supported by the National Natural Science Foundation of China(No.82071762);the Shanghai Key Lab of Human Performance(Shanghai University of Sport)(No.11DZ2261100);the 2021 Capacity Building of Shanghai Universities(No.21010503600),China。

摘　　要：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.

关 键 词：Endoplasmic reticulum-associated degradation(ERAD) Protein folding UBIQUITINATION Retrotranslocation 

分 类 号：Q24[生物学—细胞生物学] Q51