2025
Cryo-EM structure of the brine shrimp mitochondrial ATP synthase suggests an inactivation mechanism for the ATP synthase leak channel
Kumar A, da Fonseca Rezende e Mello J, Wu Y, Morris D, Mezghani I, Smith E, Rombauts S, Bossier P, Krahn J, Sigworth F, Mnatsakanyan N. Cryo-EM structure of the brine shrimp mitochondrial ATP synthase suggests an inactivation mechanism for the ATP synthase leak channel. Cell Death & Differentiation 2025, 32: 1518-1535. PMID: 40108410, PMCID: PMC12325954, DOI: 10.1038/s41418-025-01476-w.Peer-Reviewed Original ResearchMitochondrial permeability transition poreATP synthaseMammalian ATP synthaseOpening of mitochondrial permeability transition poreMitochondrial inner membraneMitochondrial ATP synthaseC-terminal regionPermeability transition poreCryo-EM structureCrustacean Artemia franciscanaSingle-particle cryo-electron microscopyCryo-electron microscopyMammalian mitochondriaAccumulate large amountsCa2+-inducedInner membraneLeak channelsOuter membranePermeability transitionTransition poreE subunitCell deathMitochondrial dysfunctionMolecular mechanismsCa2+
2020
The new role of F1Fo ATP synthase in mitochondria-mediated neurodegeneration and neuroprotection
Mnatsakanyan N, Jonas EA. The new role of F1Fo ATP synthase in mitochondria-mediated neurodegeneration and neuroprotection. Experimental Neurology 2020, 332: 113400. PMID: 32653453, PMCID: PMC7877222, DOI: 10.1016/j.expneurol.2020.113400.Peer-Reviewed Original ResearchConceptsMitochondrial inner membraneATP synthaseInner membraneOxidative phosphorylationF1Fo-ATP synthaseUnique rotational mechanismMitochondrial inner membrane potentialEfficient cellular metabolismInner membrane potentialMitochondrial permeability transition porePermeability transition poreUnique regulatorAbundant proteinsNew roleCellular metabolismCell lifeProton translocationATP synthesisTransition poreCell survivalElectrochemical gradientCertain pathophysiological conditionsSynthaseATPMembrane potential
2019
A mitochondrial megachannel resides in monomeric F1FO ATP synthase
Mnatsakanyan N, Llaguno MC, Yang Y, Yan Y, Weber J, Sigworth FJ, Jonas EA. A mitochondrial megachannel resides in monomeric F1FO ATP synthase. Nature Communications 2019, 10: 5823. PMID: 31862883, PMCID: PMC6925261, DOI: 10.1038/s41467-019-13766-2.Peer-Reviewed Original ResearchConceptsATP synthase monomersMitochondrial permeability transition poreATP synthaseGiant unilamellar vesiclesMitochondrial megachannelOligomeric stateSmall unilamellar vesiclesF1Fo-ATP synthaseMitochondrial ATP synthaseMitochondrial inner membraneCryo-EM density mapsPermeability transition porePorcine heart mitochondriaUnilamellar vesiclesInner membraneMPTP activityTransition poreElectron cryomicroscopyChannel activityLipid compositionDimer formationHeart mitochondriaSynthaseChannel formationVesicles
2017
Inhibition of Bcl-xL prevents pro-death actions of ΔN-Bcl-xL at the mitochondrial inner membrane during glutamate excitotoxicity
Park HA, Licznerski P, Mnatsakanyan N, Niu Y, Sacchetti S, Wu J, Polster BM, Alavian KN, Jonas EA. Inhibition of Bcl-xL prevents pro-death actions of ΔN-Bcl-xL at the mitochondrial inner membrane during glutamate excitotoxicity. Cell Death & Differentiation 2017, 24: 1963-1974. PMID: 28777375, PMCID: PMC5635221, DOI: 10.1038/cdd.2017.123.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsbcl-X ProteinBiphenyl CompoundsCell DeathCyclosporineGlutamic AcidMembrane Potential, MitochondrialMitochondrial MembranesMitochondrial Proton-Translocating ATPasesModels, BiologicalMutant ProteinsNeuritesNeurotoxinsNitrophenolsPiperazinesProtein SubunitsRats, Sprague-DawleyRhodaminesSulfonamidesConceptsBcl-xLABT-737ΔN-BclMitochondrial membraneWEHI-539ATP synthase c-subunitMitochondrial inner membrane depolarizationPro-death actionInner membrane depolarizationMitochondrial inner membraneOuter mitochondrial membraneMitochondrial inner membrane potentialATP synthase activityActivation of BaxInner membrane potentialMitochondrial permeability transition poreMitochondrial membrane potentialMembrane potentialPermeability transition poreAnti-apoptotic activityC subunitInner membraneB-cell lymphoma extra-large proteinBax activationGlutamate toxicityThe Mitochondrial Permeability Transition Pore: Molecular Structure and Function in Health and Disease
Jonas E, Porter G, Beutner G, Mnatsakanyan N, Park H, Mehta N, Chen R, Alavian K. The Mitochondrial Permeability Transition Pore: Molecular Structure and Function in Health and Disease. Biological And Medical Physics, Biomedical Engineering 2017, 69-105. DOI: 10.1007/978-3-319-55539-3_3.Peer-Reviewed Original ResearchMitochondrial permeability transition porePermeability transition poreCell deathTransition poreMitochondrial inner membraneInner mitochondrial membraneC subunitATP synthaseInner membraneOuter membraneMitochondrial membraneCardiac developmentRegulatory mechanismsOxidative phosphorylationATP productionMitochondrial functionMolecular componentsMitochondrial efficiencyOsmotic dysregulationCell functionLarge conductanceRecent findingsPersistent openingMembraneIon transport
2014
Impaired import: how huntingtin harms
Jonas EA. Impaired import: how huntingtin harms. Nature Neuroscience 2014, 17: 747-749. PMID: 24866036, PMCID: PMC4448962, DOI: 10.1038/nn.3726.Peer-Reviewed Original Research
2009
The role of mitochondrial uncoupling proteins in lifespan
Dietrich MO, Horvath TL. The role of mitochondrial uncoupling proteins in lifespan. Pflügers Archiv - European Journal Of Physiology 2009, 459: 269-275. PMID: 19760284, PMCID: PMC2809791, DOI: 10.1007/s00424-009-0729-0.Peer-Reviewed Original ResearchConceptsMitochondrial inner membraneCellular biochemical reactionsMitochondrial uncoupling proteinProduction of ATPCellular functionsInner membraneSpecialized proteinsBreakdown of lipidsMain organellesExcess of ROSPhysiological uncouplingOxidative phosphorylationUncoupling proteinAdenosine triphosphateOxygen reactive speciesROS productionProteinEnergetic substratesBiochemical reactionsCellular damageMitochondriaROSIntermediate substrateUCPShed light
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