Atomistic simulations indicate the c-subunit ring of the F1Fo ATP synthase is not the mitochondrial permeability transition pore
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Pathological metabolic conditions such as ischemia induce the rupture of the mitochondrial envelope and the release of pro-apoptotic proteins, leading to cell death. At the onset of this process, the inner mitochondrial membrane becomes depolarized and permeable to osmolytes, proposedly due to the opening of a non-selective protein channel of unknown molecular identity. A recent study purports that this channel, referred to as Mitochondrial Permeability Transition Pore (MPTP), is formed within the c-subunit ring of the ATP synthase, upon its dissociation from the catalytic domain of the enzyme. Here, we examine this claim for two c-rings of different lumen width, through calculations of their ion conductance and selectivity based on all-atom molecular dynamics simulations. We also quantify the likelihood that the lumen of these c-rings is in a hydrated, potentially conducting state rather than empty or blocked by lipid molecules. These calculations demonstrate that the structure and biophysical properties of a correctly assembled c-ring are inconsistent with those attributed to the MPTP.
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Very recent findings seem to exclude possibility that F1FO ATPase constitutes pore-forming component of PTPC.
“However, very recent findings seem to exclude the possibility that the F1FO ATPase constitutes the pore-forming component of the PTPC [402–405].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [404]
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- Authors
- Zhou, W., Marinelli, F., Nief, C., & Faraldo-Gómez, J. D.
- Affiliations
- National Institutes of Health (US)
- Theoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States
- Corresponding author
- Marinelli, Fabrizio
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2017-02-10
- Volume
- 6
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC5323039
- OpenAlex
- W2586483729
- Cited by
- 75
- References
- 40
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 1 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 12 · 2019: 17 · 2018: 15 · 2017: 13
- FWCI
- 6.36
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Heart, Lung, and Blood Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- mitochondrial permeability transition pore, F1FO-ATP synthase, ionic conductance, ion selectivity, mitochondrial membrane permeability, apoptosis, molecular dynamics simulation
- MeSH terms
- Mitochondrial Permeability Transition Pore, Saccharomyces cerevisiae, Mitochondrial Proton-Translocating ATPases, Mitochondrial Membrane Transport Proteins, Molecular Dynamics Simulation
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