In case of stress, hold tight: phosphorylation switches PDI from an oxidoreductase to a holdase, tuning ER proteostasis | Zendy

Coelho Joao PL | Zendy; Feige Matthias J | Zendy

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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 , phosphorylation , unfolded protein response , chemistry , oxidoreductase , microbiology and biotechnology , biology , biochemistry , endoplasmic reticulum , enzyme

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.

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