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Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities, and pathophysiological functions
Author(s) -
Wang Lei,
Yu Jiaojiao,
Wang Chihchen
Publication year - 2021
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.202000147
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , isomerase , thioredoxin , biochemistry , protein folding , chaperone (clinical) , context (archaeology) , function (biology) , microbiology and biotechnology , chemistry , biology , enzyme , biophysics , medicine , paleontology , pathology
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.