Cited by 161Mitochondrial Function and PathologyCell death mechanisms and regulationCardiac Ischemia and Reperfusion

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Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis

Tomasello, Flora, Messina, Angela, Lartigue, Lydia, Schembri, Laura, Medina, Chantal, Reina, Simona, Thoraval, Didier, Crouzet, Marc, Ichas, François, De Pinto, Vito, De Giorgi, Francesca·2009·Cell Research

DOI 10.1038/cr.2009.98

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Abstract

Voltage-dependent anion channel (VDAC)1 is the main channel of the mitochondrial outer membrane (MOM) and it has been proposed to be part of the permeability transition pore (PTP), a putative multiprotein complex candidate agent of the mitochondrial permeability transition (MPT). Working at the single live cell level, we found that overexpression of VDAC1 triggers MPT at the mitochondrial inner membrane (MIM). Conversely, silencing VDAC1 expression results in the inhibition of MPT caused by selenite-induced oxidative stress. This MOM-MIM crosstalk was modulated by Cyclosporin A and mitochondrial Cyclophilin D, but not by Bcl-2 and Bcl-X(L), indicative of PTP operation. VDAC1-dependent MPT engages a positive feedback loop involving reactive oxygen species and p38-MAPK, and secondarily triggers a canonical apoptotic response including Bax activation, cytochrome c release and caspase 3 activation. Our data thus support a model of the PTP complex involving VDAC1 at the MOM, and indicate that VDAC1-dependent MPT is an upstream mechanism playing a causal role in oxidative stress-induced apoptosis.

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Authors: Tomasello, F., Messina, A., Lartigue, L., Schembri, L., Medina, C., Reina, S., Thoraval, D., Crouzet, M., Ichas, F., De Pinto, V., & De Giorgi, F.
Affiliations: University of Catania (IT)
Inserm (FR)
Centre National de la Recherche Scientifique (FR)
ORCID: Messina, Angela
Lartigue, Lydia
Reina, Simona
Thoraval, Didier
Ichas, François
Venue: Cell Research
Publisher: Springer Science and Business Media LLC
Published: 2009-08-11
Volume: 19
Issue: 12
Pages: 1363-1376
ISSN: 1001-0602 (ISSN-L)
1748-7838
DOI: 10.1038/cr.2009.98
OpenAlex: W2054828537
Cited by: 161
References: 71
Citations by year: 2026: 11 · 2025: 13 · 2024: 7 · 2023: 5 · 2022: 4 · 2021: 8 · 2020: 13 · 2019: 7 · 2018: 7 · 2017: 12 · 2016: 11 · 2015: 11 · 2014: 14 · 2013: 8 · 2012: 8
FWCI: 4.02
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Cell Research (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: Institut National de la Santé et de la Recherche Médicale
Ligue Contre le Cancer
Università di Catania
Institut Bergonié
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
Keywords: VDAC1, mitochondrial permeability transition, mitochondrial permeability transition pore, mitochondrial outer membrane, inner mitochondrial membrane, oxidative stress-induced apoptosis, selenite, cyclosporine, cyclophilin D, reactive oxygen species, p38 MAPK, Bax activation, cytochrome c release, caspase-3
MeSH terms: Peptidyl-Prolyl Isomerase F, Animals, Cell Membrane Permeability, Chlorocebus aethiops, HeLa Cells, Humans, Stress, Physiological, Cyclosporine, Sodium Selenite, Oxidative Stress, COS Cells, Gene Silencing, Cyclophilins, Feedback, Physiological, Voltage-Dependent Anion Channel 1, Apoptosis Regulatory Proteins, Mitochondrial Membranes, Membrane Potential, Mitochondrial

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Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis

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