Distribution and Apoptotic Function of Outer Membrane Proteins Depend on Mitochondrial Fusion
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Cells deficient in mitochondrial fusion have been shown to have defects linked to the exchange of inner membrane and matrix components. Because outer-mitochondrial membrane (OMM) constituents insert directly from the cytoplasm, a role for fusion in their intermitochondrial transfer was unanticipated. Here, we show that fibroblasts lacking the GTPases responsible for OMM fusion, mitofusins 1 and 2 (MFN1 and MFN2), display more heterogeneous distribution of OMM proteins. Proteins with different modes of OMM association display varying degrees of heterogeneity in Mfn1/2(-/-) cells and different kinetics of transfer during fusion in fusion-competent cells. Proapoptotic Bak exhibits marked heterogeneity, which is normalized upon expression of MFN2. Bak is critical for Bid-induced OMM permeabilization and cytochrome c release, and Mfn1/2(-/-) cells show dysregulation of Bid-dependent apoptotic signaling. Bid sensitivity of Bak-deficient mitochondria is regained upon fusion with Bak-containing mitochondria. Thus, OMM protein distribution depends on mitochondrial fusion and is a locus of apoptotic dysfunction in conditions of fusion deficiency.
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Mitochondrial size and shape as well as lipid composition can influence the likelihood of mitochondria to undergo irreversible MOMP.
“Finally, it is becoming increasingly evident that mitochondrial size and shape [139–141] as well as lipid composition [142, 143] can influence the likelihood of mitochondria to undergo irreversible MOMP.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [141]
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- Authors
- Weaver, D., Eisner, V., Liu, X., Várnai, P., Hunyady, L., Gross, A., & Hajnóczky, G.
- Affiliations
- Thomas Jefferson University (US)
- Semmelweis University (HU)
- Weizmann Institute of Science (IL)
- Corresponding author
- Hajnóczky, György
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 54
- Issue
- 5
- Pages
- 870-878
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC4363113
- OpenAlex
- W2062535484
- Cited by
- 58
- References
- 55
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 1 · 2023: 5 · 2022: 5 · 2021: 7 · 2020: 1 · 2019: 6 · 2018: 5 · 2017: 7 · 2016: 6 · 2015: 5 · 2014: 3
- FWCI
- 2.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Semmelweis University Repository (Semmelweis University) (submittedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (R01AA017773)
- National Cancer Institute (P30CA056036)
- National Institute of General Medical Sciences (R01GM059419)
- 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 › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial fusion, mitochondrial outer membrane, mitofusins, Mfn1, mitofusin 2, Bak, Bid, apoptosis, cytochrome c release, mitochondrial permeability transition, fibroblasts
- MeSH terms
- Animals, Cell Line, Humans, Muscle Fibers, Skeletal, GTP Phosphohydrolases, Protein Transport, Mitochondrial Proteins, Voltage-Dependent Anion Channel 2, bcl-2 Homologous Antagonist-Killer Protein, BH3 Interacting Domain Death Agonist Protein, Mitochondrial Membranes, Mice, Rats, Gene Knockout Techniques, Mitochondrial Dynamics
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