2023
Mitochondrial DNA and the STING pathway are required for hepatic stellate cell activation
Arumugam S, Li B, Boodapati S, Nathanson M, Sun B, Ouyang X, Mehal W. Mitochondrial DNA and the STING pathway are required for hepatic stellate cell activation. Hepatology 2023, 78: 1448-1461. PMID: 37013923, PMCID: PMC10804318, DOI: 10.1097/hep.0000000000000388.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelBioenergetic capacityMitochondrial DNATranscriptional upregulationCyclic GMP-AMP synthaseGMP-AMP synthaseTranscriptional regulationBioenergetic organellesFunctional mitochondriaMitochondrial membraneExternal mitochondrial membraneAnabolic pathwaysMitochondrial massAnion channelInterferon genesHSC transdifferentiationSubsequent activationCGAS-STINGTransdifferentiationIRF3 pathwayPathwaySTING pathwayGenesMitochondriaQuiescent HSCs
2022
Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein–VDAC complexation as a potential therapeutic target for Parkinson’s disease treatment
Rajendran M, Queralt-Martín M, Gurnev P, Rosencrans W, Rovini A, Jacobs D, Abrantes K, Hoogerheide D, Bezrukov S, Rostovtseva T. Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein–VDAC complexation as a potential therapeutic target for Parkinson’s disease treatment. Cellular And Molecular Life Sciences 2022, 79: 368. PMID: 35718804, PMCID: PMC11072225, DOI: 10.1007/s00018-022-04389-w.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelVDAC poreProtein-membrane bindingRegulating mitochondrial functionProximity ligation assayInvolvement of alpha-synucleinMembrane bindingMitochondrial respirationMitochondrial functionHeLa cellsLigation assayLipid membranesHexokinase 2MitochondriaTranslocation processComplex inhibitionAnion channelFluorescence correlation spectroscopyAlpha-synucleinMolecular levelMitochondrial toxicityASynTranslocationPeptide therapeuticsTherapeutic target
2020
Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations
Hoogerheide D, Rostovtseva T, Jacobs D, Gurnev P, Bezrukov S. Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations. ACS Nano 2020, 15: 989-1001. PMID: 33369404, PMCID: PMC9019845, DOI: 10.1021/acsnano.0c07672.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelMembrane surfaceSingle-molecule levelSame membrane surfaceIndividual proteinsAnion channelNeuronal proteinsLipid membranesBinding conformationsLipid surfaceLipid compositionProteinΑ-synucleinMembraneConformationOrders of magnitudeSurfaceUnbindingMitochondriaBindsObserved distributionNanoporesMoleculesΑSynTrapsA lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology
Queralt-Martín M, Bergdoll L, Teijido O, Munshi N, Jacobs D, Kuszak A, Protchenko O, Reina S, Magrì A, De Pinto V, Bezrukov S, Abramson J, Rostovtseva T. A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology. Journal Of General Physiology 2020, 152: e201912501. PMID: 31935282, PMCID: PMC7062508, DOI: 10.1085/jgp.201912501.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelCysteine residuesMitochondrial outer membraneGeneral molecular mechanismIsoform-specific functionsHigh sequence similarityCysteine-scanning mutagenesisIsoform-specific rolesIsoform-specific regulationUnique functional rolesMitochondrial biologyVDAC isoformsMetabolite exchangeOuter membraneScanning mutagenesisCytosolic proteinsΑ-synucleinAnion channelVoltage-gated channelsMolecular mechanismsMitochondrial bioenergeticsProtein α-synucleinVDAC3VDAC1Functional role
2018
Assessing the role of residue E73 and lipid headgroup charge in VDAC1 voltage gating
Queralt-Martín M, Bergdoll L, Jacobs D, Bezrukov S, Abramson J, Rostovtseva T. Assessing the role of residue E73 and lipid headgroup charge in VDAC1 voltage gating. Biochimica Et Biophysica Acta (BBA) - Bioenergetics 2018, 1860: 22-29. PMID: 30412693, PMCID: PMC8283775, DOI: 10.1016/j.bbabio.2018.11.001.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelMitochondrial outer membraneVoltage gatingVoltage-gating processCholesterol binding siteVDAC's roleVDAC functionGating processMetabolite transportOuter membraneAbundant proteinsMOM permeabilityVDAC gatingPlanar lipid membranesAnion channelE73Mitochondrial respirationLipid bilayer systemsLipid headgroup chargeBinding sitesLipid membranesPhospholipid headgroupsElectrophysiology measurementsTransport of ionsRecent studies
2011
Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum
Bouyer G, Cueff A, Egée S, Kmiecik J, Maksimova Y, Glogowska E, Gallagher PG, Thomas SL. Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum. Blood 2011, 118: 2305-2312. PMID: 21795748, DOI: 10.1182/blood-2011-01-329300.Peer-Reviewed Original ResearchConceptsPeripheral-type benzodiazepine receptorBenzodiazepine receptorsNew permeability pathwaysP falciparumPlasmodium falciparumFalciparum-infected erythrocytesAnti-malarial therapyP falciparum-infected erythrocytesErythrocyte membranesInfected erythrocytesAnion channelIntraerythrocytic growthFalciparumReceptorsSelective inhibitionEndogenous channelsVoltage-dependent anion channelPharmacologic applicationsPermeability pathwaysErythrocytesMolecular identityObvious targetTherapy
2006
Zinc-Dependent Multi-Conductance Channel Activity in Mitochondria Isolated from Ischemic Brain
Bonanni L, Chachar M, Jover-Mengual T, Li H, Jones A, Yokota H, Ofengeim D, Flannery RJ, Miyawaki T, Cho CH, Polster BM, Pypaert M, Hardwick JM, Sensi SL, Zukin RS, Jonas EA. Zinc-Dependent Multi-Conductance Channel Activity in Mitochondria Isolated from Ischemic Brain. Journal Of Neuroscience 2006, 26: 6851-6862. PMID: 16793892, PMCID: PMC4758341, DOI: 10.1523/jneurosci.5444-05.2006.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternBrain IschemiaCaspasesChelating AgentsDiagnostic ImagingDose-Response Relationship, DrugEthylenediaminesIon Channel GatingIon ChannelsMaleMembrane PotentialsMicroscopy, Electron, TransmissionMitochondriaNADPatch-Clamp TechniquesRatsRats, Sprague-DawleySynaptosomesXanthenesZincConceptsVoltage-dependent anion channelOuter mitochondrial membraneMitochondrial membraneChannel activityMitochondrial outer membraneMitochondrial channel activity
2004
Proapoptotic 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
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply