2012
Multipolar functions of BCL-2 proteins link energetics to apoptosis
Hardwick JM, Chen YB, Jonas EA. Multipolar functions of BCL-2 proteins link energetics to apoptosis. Trends In Cell Biology 2012, 22: 318-328. PMID: 22560661, PMCID: PMC3499971, DOI: 10.1016/j.tcb.2012.03.005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCaspasesEvolution, MolecularHumansMitochondrial MembranesProto-Oncogene Proteins c-bcl-2ConceptsBcl-2 proteinClassical apoptotic cell deathBcl-2 family proteinsSub-mitochondrial localizationApoptotic cell deathFamily proteinsClassical apoptosisBiochemical activityApoptosis regulatorCritical crosstalkCell survivalCell deathProteinApoptosisProfound effectCellsMultipolar functionsRegulatorCrosstalkLocalizationCurrent assumptionsDeath
2009
Molecular participants in mitochondrial cell death channel formation during neuronal ischemia
Jonas EA. Molecular participants in mitochondrial cell death channel formation during neuronal ischemia. Experimental Neurology 2009, 218: 203-212. PMID: 19341732, PMCID: PMC2710418, DOI: 10.1016/j.expneurol.2009.03.025.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell Membrane PermeabilityHumansIon ChannelsIschemiaMitochondriaMitochondrial MembranesNeuronsProto-Oncogene Proteins c-bcl-2Voltage-Dependent Anion ChannelsConceptsBcl-2 family proteinsCell deathFamily proteinsInner membraneOuter membraneIon channelsMolecular participantsNumerous cellular processesMitochondrial ion channelsComplex of proteinsSpecialized physiological functionsMembrane compartmentalizationIon channel complexCellular processesPhysiological functionsIon channel conductanceCytosolic metabolitesChannel complexProteinMembrane potentialChannel formationMembraneChannel conductanceSynaptic transmissionVDAC
2005
The Role of the Mitochondrial Apoptosis Induced Channel MAC in Cytochrome c Release
Martinez-Caballero S, Dejean LM, Jonas EA, Kinnally KW. The Role of the Mitochondrial Apoptosis Induced Channel MAC in Cytochrome c Release. Journal Of Bioenergetics And Biomembranes 2005, 37: 155-164. PMID: 16167172, DOI: 10.1007/s10863-005-6570-z.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCytochromes cHumansIon ChannelsMiceMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial MembranesMitochondrial Permeability Transition PoreProto-Oncogene Proteins c-bcl-2ConceptsMitochondrial apoptosis-induced channelBcl-2 family proteinsMitochondrial outer membraneCytochrome cOuter membrane integrityCytochrome c releaseHigh-conductance channelPermeability transition poreIntermembrane spaceFamily proteinsCommitment stepOuter membraneC releaseProapoptotic factorsTransition poreSingle-channel behaviorMAC formationMembrane integrityCrucial eventEarly apoptosisApoptosisMolecular compositionRelease channelMAC activityMitochondriaOligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel
Dejean LM, Martinez-Caballero S, Guo L, Hughes C, Teijido O, Ducret T, Ichas F, Korsmeyer SJ, Antonsson B, Jonas EA, Kinnally KW. Oligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel. Molecular Biology Of The Cell 2005, 16: 2424-2432. PMID: 15772159, PMCID: PMC1087246, DOI: 10.1091/mbc.e04-12-1111.Peer-Reviewed Original ResearchConceptsMitochondrial apoptosis-induced channelOligomeric BaxBcl-2 family proteinsHeLa cellsBcl-2-overexpressing cellsCytochrome cChannel activityMAC activityIntrinsic apoptotic pathwayApoptotic cellsFamily proteinsIntrinsic apoptosisApoptotic pathwaySingle-channel behaviorMitochondriaBaxBax antibodiesMean conductanceBakUntreated cellsRelease channelProteinApoptosisCellsTranslocation
2004
Exposure to Hypoxia Rapidly Induces Mitochondrial Channel Activity within a Living Synapse*
Jonas EA, Hickman JA, Hardwick JM, Kaczmarek LK. Exposure to Hypoxia Rapidly Induces Mitochondrial Channel Activity within a Living Synapse*. Journal Of Biological Chemistry 2004, 280: 4491-4497. PMID: 15561723, DOI: 10.1074/jbc.m410661200.Peer-Reviewed Original ResearchConceptsMitochondrial channel activityMitochondrial membraneChannel activityBcl-xLBcl-2 family proteinsPro-apoptotic fragmentsOuter mitochondrial membraneTrigger cell deathZ-VAD-FMKBenzyloxycarbonyl-VADFamily proteinsSynaptic responsesMulticonductance channelLarge conductance channelFluoromethyl ketoneCell deathMinutes of hypoxiaResponses of neuronsNeuronal functionSquid giant synapseSynaptic mitochondriaEarly eventsSynaptic functionHypoxic conditionsNeuronal deathProapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals
Jonas EA, Hickman JA, Chachar M, Polster BM, Brandt TA, Fannjiang Y, Ivanovska I, Basañez G, Kinnally KW, Zimmerberg J, Hardwick JM, Kaczmarek LK. Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 13590-13595. PMID: 15342906, PMCID: PMC518799, DOI: 10.1073/pnas.0401372101.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBcl-X ProteinDecapodiformesElectric ConductivityEndopeptidasesHypoxiaIon ChannelsLiposomesMitochondriaNADPatch-Clamp TechniquesPorinsPresynaptic TerminalsProtein Processing, Post-TranslationalProto-Oncogene Proteins c-bcl-2Sequence DeletionVoltage-Dependent Anion ChannelsConceptsBcl-xLMitochondrial channelsDeath pathwaysMitochondrial membraneBcl-xL.Proapoptotic Bcl-2 family proteinsVoltage-dependent anion channelBcl-2 family proteinsOuter mitochondrial membraneCell death pathwaysHydrophobic C-terminusBcl-xL proteinAntiapoptotic Bcl-xLNeuronal death pathwaysDeath stimuliBH3 domainFamily proteinsSquid presynaptic terminalsMammalian cellsC-terminusAnion channelMitochondriaChannel activityOpposite effectHealthy neuronsRegulation of Synaptic Transmission by Mitochondrial Ion Channels
Jonas E. Regulation of Synaptic Transmission by Mitochondrial Ion Channels. Journal Of Bioenergetics And Biomembranes 2004, 36: 357-361. PMID: 15377872, DOI: 10.1023/b:jobb.0000041768.11006.90.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBcl-X ProteinCell HypoxiaCell MembraneDecapodiformesElectric ConductivityHomeostasisHumansIon Channel GatingIon ChannelsMembrane PotentialsMitochondriaMitochondrial ProteinsNeuronsOxidative StressPorinsProto-Oncogene Proteins c-bcl-2Synaptic TransmissionVoltage-Dependent Anion ChannelsConceptsMitochondrial outer membraneVoltage-dependent anion channelOuter membraneBcl-xLSynaptic transmissionChannel activityNeuronal presynaptic terminalsMitochondrial ion channelsProteolytic fragmentsBcl-xL proteinRelease of ATPIon channel activityPresynaptic terminalsRapid onsetSynaptic functionNeurotransmitter releaseBcl-xL.Anion channelNeurotransmitter secretionPrevents cleavageHypoxiaIon channelsProtease inhibitorsLarge conductanceMitochondria
2003
Modulation of Synaptic Transmission by the BCL-2 Family Protein BCL-xL
Jonas EA, Hoit D, Hickman JA, Brandt TA, Polster BM, Fannjiang Y, McCarthy E, Montanez MK, Hardwick JM, Kaczmarek LK. Modulation of Synaptic Transmission by the BCL-2 Family Protein BCL-xL. Journal Of Neuroscience 2003, 23: 8423-8431. PMID: 12968005, PMCID: PMC6740692, DOI: 10.1523/jneurosci.23-23-08423.2003.Peer-Reviewed Original ResearchConceptsBcl-2 family proteinsProtein Bcl-xLBcl-xLFamily proteinsMitochondrial membranePro-apoptotic cleavage productRecombinant Bcl-xLBcl-xL proteinMitochondrial calcium uptakePresynaptic terminalsInfluences synaptic transmissionCell deathGiant presynaptic terminalSynaptic transmissionChannel activityProteinSquid stellate ganglionMitochondriaCleavage productsSynaptic stabilityAdult brainPostsynaptic responsesCalcium uptakeMembranePatch pipette