蛋白质二硫键异构酶
内质网
异构酶
生物化学
蛋白质折叠
硫氧还蛋白
伴侣(临床)
背景(考古学)
细胞生物学
化学
功能(生物学)
生物
酶
生物物理学
医学
病理
古生物学
作者
Lei Wang,Jiaojiao Yu,Chih‐Chen Wang
出处
期刊:BioEssays
[Wiley]
日期:2020-11-06
卷期号:43 (3)
被引量:20
标识
DOI:10.1002/bies.202000147
摘要
Abstract Protein disulfide isomerase (PDI) is one of the most abundant and critical protein folding catalysts in the endoplasmic reticulum of eukaryotic cells. PDI consists of four thioredoxin domains and interacts with a wide range of substrate and partner proteins due to its intrinsic conformational flexibility. PDI plays multifunctional roles in a variety of pathophysiological events, both as an oxidoreductase and a molecular chaperone. Recent studies have revealed that the conformation and activity of PDI can be regulated in multiple ways, including posttranslational modification and substrate/ligand binding. Here, we summarize recent advances in understanding the function and regulation of PDI in different pathological and physiological events. We propose that the multifunctional roles of PDI are regulated by multiple mechanisms. Furthermore, we discuss future directions for the study of PDI, emphasizing how different regulatory modes are linked to the conformational changes and biological functions of PDI in the context of diverse pathophysiologies.
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