2023
Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions
Bernardi P, Gerle C, Halestrap A, Jonas E, Karch J, Mnatsakanyan N, Pavlov E, Sheu S, Soukas A. Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions. Cell Death & Differentiation 2023, 30: 1869-1885. PMID: 37460667, PMCID: PMC10406888, DOI: 10.1038/s41418-023-01187-0.Peer-Reviewed Original ResearchConceptsMitochondrial permeability transition poreMitochondrial permeability transitionAdenine nucleotide translocasePermeability transition poreATP synthase dimersTransition poreInner mitochondrial membrane permeabilityC subunit ringOuter mitochondrial membraneMitochondrial membrane permeabilityDeath of cellsMPTP openingNecrotic cell deathMitochondrial membraneNucleotide translocaseTransient mPTP openingMitochondrial bioenergeticsSub-conductance statesMolecular identityPermeability transitionCell deathPhysiological roleNon-selective channelsDiscovery decadesMembrane permeability
2018
Cardiac metabolic effects of KNa1.2 channel deletion and evidence for its mitochondrial localization
Smith CO, Wang YT, Nadtochiy SM, Miller JH, Jonas EA, Dirksen RT, Nehrke K, Brookes PS. Cardiac metabolic effects of KNa1.2 channel deletion and evidence for its mitochondrial localization. The FASEB Journal 2018, 32: 6135-6149. PMID: 29863912, PMCID: PMC6181635, DOI: 10.1096/fj.201800139r.Peer-Reviewed Original ResearchCardiac metabolic effectsMetabolic effectsChannel deletionCardiac ischemia-reperfusion injuryIschemia-reperfusion injuryWild-type miceCardiac metabolomeBaseline differencesBody fatVolatile anestheticsElectrophysiological evidenceMiceKCNT2Physiological roleCardiomyocytesFatMembrane preparationsMolecular identityCardioprotectionEvidenceInjuryMitochondrial localizationAnesthetics
2014
An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore
Alavian KN, Beutner G, Lazrove E, Sacchetti S, Park HA, Licznerski P, Li H, Nabili P, Hockensmith K, Graham M, Porter GA, Jonas EA. An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 10580-10585. PMID: 24979777, PMCID: PMC4115574, DOI: 10.1073/pnas.1401591111.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCell DeathHEK293 CellsHumansIon Channel GatingIon ChannelsLiposomesMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial MembranesMitochondrial Permeability Transition PoreMutationProtein ConformationProtein SubunitsProton-Translocating ATPasesRatsReactive Oxygen SpeciesConceptsMitochondrial PT poreF1Fo-ATP synthaseATP synthasePermeability transitionCell deathCellular metabolic efficiencyInner mitochondrial membrane permeabilityOxygen species-induced cell deathC subunit ringATP synthase F1Mitochondrial membrane permeabilityMitochondrial permeability transitionC subunitPT poreTight regulationATP productionMolecular identitySingle-channel conductanceChannel closureLeak channelsMPTP openingMetabolic efficiencyMembrane permeabilityHealthy cellsOsmotic shifts
2004
Ion channels on intracellular organelles
Kaczmarek L, Jonas E. Ion channels on intracellular organelles. Advances In Molecular And Cell Biology 2004, 32: 433-458. DOI: 10.1016/s1569-2558(03)32018-1.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsExternal signalsIon channelsCellular functionsInner membraneMitochondrial channelsIntracellular membranesPlasma membraneIntracellular organellesMolecular identityCell deathCytoplasmic calcium levelsHandling of calciumRyanodine receptorProperties of channelsCytoplasmic calciumIntracellular storesPotential roleRelease of calciumInternal storesMembraneRegulationKey roleSynaptic transmissionCalcium influxIntracellular calcium