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

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 enzym...

Full description

Saved in:
Bibliographic Details
Published inThe EMBO journal Vol. 39; no. 10; pp. e104880 - n/a
Main Authors Coelho, Joao PL, Feige, Matthias J
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 18.05.2020
Blackwell Publishing Ltd
John Wiley and Sons Inc
Subjects
EMBO20
EMBO31
EMBO32
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Homeostasis
News & Views
Oxidoreductase
Oxidoreductases - metabolism
Phosphorylation
Protein disulfide-isomerase
Protein Disulfide-Isomerases - metabolism
Protein folding
Proteostasis
Stress response
Switches
Views
Online AccessGet full text

Cover

More Information
Summary: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. Graphical Abstract A new study reveals that the chaperone activity of protein disulfide isomerase is reversibly modulated to protect cells against acute ER stress.
Bibliography:SourceType-Other Sources-1
ObjectType-News-1
ObjectType-Commentary-2
content type line 66
See also: https://doi.org/10.15252/embj.2019103841 (May 2020)
ISSN:0261-4189
1460-2075
DOI:10.15252/embj.2020104880