The V-ATPase/ATG16L1 axis is controlled by the V

ATG16L1 ATP6V1H CASM STING V-ATPase VAIL autophagy influenza non-canonical autophagy vacuolar ATPase

Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
24 Jul 2024
Historique:
received: 18 12 2023
revised: 15 05 2024
accepted: 05 07 2024
medline: 2 8 2024
pubmed: 2 8 2024
entrez: 1 8 2024
Statut: aheadofprint

Résumé

Defects in organellar acidification indicate compromised or infected compartments. Recruitment of the autophagy-related ATG16L1 complex to pathologically neutralized organelles targets ubiquitin-like ATG8 molecules to perturbed membranes. How this process is coupled to proton gradient disruption is unclear. Here, we reveal that the V

Identifiants

DOI: 10.1016/j.molcel.2024.07.003 PMID: 39089251
pubmed: 39089251
pii: S1097-2765(24)00579-3
doi: 10.1016/j.molcel.2024.07.003
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

Auteurs

Lewis Timimi (L)

Cell Biology of Infection Laboratory, The Francis Crick Institute, London NW1 1AT, UK; Division of Medicine, University College London, London WC1E 6JF, UK.

Antoni G Wrobel (AG)

Structural Biology of Disease Processes Laboratory, The Francis Crick Institute, London NW1 1AT, UK; Structural Biology STP, The Francis Crick Institute, London NW1 1AT, UK.

George N Chiduza (GN)

Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Sarah L Maslen (SL)

Proteomics STP, The Francis Crick Institute, London NW1 1AT, UK.

Antonio Torres-Méndez (A)

Neural Circuits & Evolution Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Beatriz Montaner (B)

Cell Biology of Infection Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Colin Davis (C)

Cellular Degradation Systems Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Taylor Minckley (T)

Neural Circuit Bioengineering and Disease Modelling Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Katriona L Hole (KL)

Mitochondrial Neurobiology Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Andrea Serio (A)

Neural Circuit Bioengineering and Disease Modelling Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Michael J Devine (MJ)

Mitochondrial Neurobiology Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

J Mark Skehel (JM)

Proteomics STP, The Francis Crick Institute, London NW1 1AT, UK.

John L Rubinstein (JL)

Molecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada; Department of Biochemistry, The University of Toronto, Toronto, ON M5S 1A8, Canada; Department of Medical Biophysics, The University of Toronto, Toronto, ON M5G 1L7, Canada.

Anne Schreiber (A)

Cellular Degradation Systems Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Rupert Beale (R)

Cell Biology of Infection Laboratory, The Francis Crick Institute, London NW1 1AT, UK; Division of Medicine, University College London, London WC1E 6JF, UK. Electronic address: rupert.beale@crick.ac.uk.

Classifications MeSH