Homeostasis of the ER redox state subsequent to proteasome inhibition.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
21 04 2021
21 04 2021
Historique:
received:
08
09
2020
accepted:
07
04
2021
entrez:
22
4
2021
pubmed:
23
4
2021
medline:
16
11
2021
Statut:
epublish
Résumé
Endoplasmic reticulum (ER) maintains within, an oxidative redox state suitable for disulfide bond formation. We monitored the ER redox dynamics subsequent to proteasome inhibition using an ER redox probe ERroGFP S4. Proteasomal inhibition initially led to oxidation of the ER, but gradually the normal redox state was recovered that further led to a reductive state. These events were found to be concomitant with the increase in the both oxidized and reduced glutathione in the microsomal fraction, with a decrease of total intracellular glutathione. The ER reduction was suppressed by pretreatment of a glutathione synthesis inhibitor or by knockdown of ATF4, which induces glutathione-related genes. These results suggested cellular adaptation of ER redox homeostasis: (1) inhibition of proteasome led to accumulation of misfolded proteins and oxidative state in the ER, and (2) the oxidative ER was then reduced by ATF4 activation, followed by influx of glutathione into the ER.
Identifiants
pubmed: 33883613
doi: 10.1038/s41598-021-87944-y
pii: 10.1038/s41598-021-87944-y
pmc: PMC8060268
doi:
Substances chimiques
Fluorescent Dyes
0
Molecular Probes
0
Proteasome Endopeptidase Complex
EC 3.4.25.1
Glutathione
GAN16C9B8O
Dimethyl Sulfoxide
YOW8V9698H
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8655Références
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