Cited by 220Cell death mechanisms and regulationMitochondrial Function and PathologyAutophagy in Disease and Therapy

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Mitochondrial Shape Governs BAX-Induced Membrane Permeabilization and Apoptosis

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Renault, Thibaud T., Floros, Konstantinos V., Elkholi, Rana, Corrigan, Kelly-Ann, Kushnareva, Yulia, Wieder, Shira Y., Lindtner, Claudia, Serasinghe, Madhavika N., Asciolla, James J., Buettner, Christoph, Newmeyer, Donald D., Chipuk, Jerry E.·2015·Molecular Cell

DOI 10.1016/j.molcel.2014.10.028PMC PMC4289414

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Abstract

Proapoptotic BCL-2 proteins converge upon the outer mitochondrial membrane (OMM) to promote mitochondrial outer membrane permeabilization (MOMP) and apoptosis. Here we investigated the mechanistic relationship between mitochondrial shape and MOMP and provide evidence that BAX requires a distinct mitochondrial size to induce MOMP. We utilized the terminal unfolded protein response pathway to systematically define proapoptotic BCL-2 protein composition after stress and then directly interrogated their requirement for a productive mitochondrial size. Complementary biochemical, cellular, in vivo, and ex vivo studies reveal that Mfn1, a GTPase involved in mitochondrial fusion, establishes a mitochondrial size that is permissive for proapoptotic BCL-2 family function. Cells with hyperfragmented mitochondria, along with size-restricted OMM model systems, fail to support BAX-dependent membrane association and permeabilization due to an inability to stabilize BAXα9·membrane interactions. This work identifies a mechanistic contribution of mitochondrial size in dictating BAX activation, MOMP, and apoptosis.

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Authors: Renault, T. T., Floros, K. V., Elkholi, R., Corrigan, K.-A., Kushnareva, Y., Wieder, S. Y., Lindtner, C., Serasinghe, M. N., Asciolla, J. J., Buettner, C., Newmeyer, D. D., & Chipuk, J. E.
Affiliations: Tisch Cancer Institute (US)
Icahn School of Medicine at Mount Sinai (US)
La Jolla Institute for Immunology (US)
Mount Sinai Hospital (US)
Corresponding author: Chipuk, Jerry E.
ORCID: Renault, Thibaud T.
Floros, Konstantinos V.
Kushnareva, Yulia
Wieder, Shira Y.
Buettner, Christoph
Newmeyer, Donald D.
Chipuk, Jerry E.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2015-01
Volume: 57
Issue: 1
Pages: 69-82
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2014.10.028
PMC: PMC4289414
OpenAlex: W2049807952
Cited by: 217
References: 51
Citations by year: 2026: 13 · 2025: 11 · 2024: 13 · 2023: 14 · 2022: 20 · 2021: 23 · 2020: 22 · 2019: 21 · 2018: 18 · 2017: 23 · 2016: 24 · 2015: 15
FWCI: 8.48
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 372 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Rutgers University Community Repository (Rutgers University) (submittedVersion)
Funders: National Institutes of Health (5r01aa023416-04)
National Institute on Alcohol Abuse and Alcoholism (NIH P20AA017067, P20AA017067, R01-AA-023416)
National Cancer Institute (CA157740, R01CA157740)
National Institute of Diabetes and Digestive and Kidney Diseases (DK083568, R03DK082724, K08DK074873, DK-082724)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: mitochondrial morphology, mitochondrial size, Bax, mitochondrial outer membrane permeabilization, apoptosis, Bcl-2 family proteins, Mfn1, mitochondrial fusion, mitochondrial outer membrane
MeSH terms: Bcl-2-Like Protein 11, Animals, Gene Expression Regulation, Membrane Proteins, Mitochondria, Liver, Permeability, Proto-Oncogene Proteins, Signal Transduction, Apoptosis, GTP Phosphohydrolases, bcl-2 Homologous Antagonist-Killer Protein, Apoptosis Regulatory Proteins, bcl-2-Associated X Protein, Mitochondrial Membranes, Mice, Membrane Potential, Mitochondrial, Organelle Shape, Unilamellar Liposomes, Mitochondrial Dynamics

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Mitochondrial Shape Governs BAX-Induced Membrane Permeabilization and Apoptosis

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