期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 43, 期 8, 页码 593-605出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2018.06.005
关键词
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资金
- NIH [R01 GM113188, R01 DK105393, R01 DK111174]
- University of Michigan Protein Folding Diseases Initiative
- Juvenile Diabetes Research Foundation (JDRF) [2-SRA-2018-539-A-B]
- American Diabetes Association (ADA) [1-12-CD-04]
- ADA
Endoplasmic reticulum (ER)-associated degradation (ERAD) and the unfolded protein response (UPR) are two key quality-control machineries in the cell. ERAD is responsible for the clearance of misfolded proteins in the ER for cytosolic proteasomal degradation, while UPR is activated in response to the accumulation of misfolded proteins. It has long been thought that ERAD is an integral part of UPR because expression of many ERAD genes is controlled by UPR; however, recent studies have suggested that ERAD has a direct role in controlling the protein turnover and abundance of IRE1 alpha, the most conserved UPR sensor. Here, we review recent advances in our understanding of IRE1 alpha activation and propose that UPR and ERAD engage in an intimate crosstalk to define folding capacity and maintain homeostasis in the ER.
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