ER Stress-Induced Sphingosine-1-Phosphate Lyase Phosphorylation Potentiates the Mitochondrial Unfolded Protein Response.
adaptive stress response
endoplasmic reticulum
endoribonuclease
eukaryotic translation initiation factor 2α
inositol-requiring enzyme-1
ire1-spl axis
kinase
mitochondria
proteostasis
signaling networks
Journal
Journal of lipid research
ISSN: 1539-7262
Titre abrégé: J Lipid Res
Pays: United States
ID NLM: 0376606
Informations de publication
Date de publication:
Oct 2022
Oct 2022
Historique:
received:
01
02
2022
revised:
29
08
2022
accepted:
01
09
2022
pubmed:
14
9
2022
medline:
26
10
2022
entrez:
13
9
2022
Statut:
ppublish
Résumé
The unfolded protein response (UPR) is an elaborate signaling network that evolved to maintain proteostasis in the endoplasmic reticulum (ER) and mitochondria (mt). These organelles are functionally and physically associated, and consequently, their stress responses are often intertwined. It is unclear how these two adaptive stress responses are coordinated during ER stress. The inositol-requiring enzyme-1 (IRE1), a central ER stress sensor and proximal regulator of the UPR
Identifiants
pubmed: 36100091
pii: S0022-2275(22)00112-2
doi: 10.1016/j.jlr.2022.100279
pmc: PMC9579414
pii:
doi:
Substances chimiques
sphingosine 1-phosphate lyase (aldolase)
EC 4.1.2.27
RNA, Double-Stranded
0
Endoribonucleases
EC 3.1.-
Protein Serine-Threonine Kinases
EC 2.7.11.1
Aldehyde-Lyases
EC 4.1.2.-
Ribonucleases
EC 3.1.-
Inositol
4L6452S749
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100279Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of Interest The authors declare that they have no conflicts of interest with the contents of this article.