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
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

100279

Informations 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.

Auteurs

Asli D Yildirim (AD)

Smidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA; Department of Molecular Biology and Genetics, Bilkent University, Ankara, Turkey; National Nanotechnology Center, Bilkent University, Ankara, Turkey.

Mevlut Citir (M)

Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.

Asli E Dogan (AE)

Smidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA; Department of Molecular Biology and Genetics, Bilkent University, Ankara, Turkey; National Nanotechnology Center, Bilkent University, Ankara, Turkey.

Zehra Veli (Z)

National Nanotechnology Center, Bilkent University, Ankara, Turkey.

Zehra Yildirim (Z)

Smidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA; Department of Molecular Biology and Genetics, Bilkent University, Ankara, Turkey; National Nanotechnology Center, Bilkent University, Ankara, Turkey.

Ozlem Tufanli (O)

New York University, Langone Medical Center, New York, NY, USA.

Alexis Traynor-Kaplan (A)

Department of Medicine, Washington University School of Medicine, Seattle, USA; ATK Innovation, Analytics and Discovery, North Bend, WA, USA.

Carsten Schultz (C)

Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, USA.

Ebru Erbay (E)

Smidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA; Department of Biomedical Sciences, Cedars-Sinai Medical Center, Los Angeles, CA, USA; David Geffen School of Medicine, University of California, Los Angeles, CA, USA. Electronic address: ebru.erbay@cshs.org.

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Classifications MeSH