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 ResearchMeSH KeywordsAlpha-SynucleinHeLa CellsHumansLipidsMitochondriaParkinson DiseaseVoltage-Dependent Anion ChannelsConceptsVoltage-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
A 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. The Journal Of General Physiology 2020, 152: e201912501. PMID: 31935282, PMCID: PMC7062508, DOI: 10.1085/jgp.201912501.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiologyCysteineCytosolHumansMiceMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial ProteinsProtein IsoformsSynucleinsVoltage-Dependent Anion Channel 1Voltage-Dependent Anion ChannelsConceptsVoltage-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
2019
Probing Membrane Association of α-Synuclein Domains with VDAC Nanopore Reveals Unexpected Binding Pattern
Jacobs D, Hoogerheide D, Rovini A, Jiang Z, Lee J, Rostovtseva T, Bezrukov S. Probing Membrane Association of α-Synuclein Domains with VDAC Nanopore Reveals Unexpected Binding Pattern. Scientific Reports 2019, 9: 4580. PMID: 30872688, PMCID: PMC6418135, DOI: 10.1038/s41598-019-40979-8.Peer-Reviewed Original Research