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In case of stress, hold tight: phosphorylation switches PDI from an oxidoreductase to a holdase, tuning ER proteostasis
Author(s) -
Coelho Joao PL,
Feige Matthias J
Publication year - 2020
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2020104880
Subject(s) - proteostasis , biology , phosphorylation , oxidoreductase , unfolded protein response , microbiology and biotechnology , biochemistry , enzyme , endoplasmic reticulum
Eukaryotic cells have evolved multiple responses that allow endoplasmic reticulum ( ER ) homeostasis to be maintained even in the face of acute or chronic stresses. In this issue, Yu et al (2020) describe how site‐specific phosphorylation switches protein disulfide isomerase ( PDI ) from a folding enzyme to a holdase chaperone which regulates ER stress responses, thus highlighting PDI as a key player in ER homeostasis.