2024
Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel
Rostovtseva T, Weinrich M, Jacobs D, Rosencrans W, Bezrukov S. Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel. International Journal Of Molecular Sciences 2024, 25: 2204. PMID: 38396879, PMCID: PMC10889239, DOI: 10.3390/ijms25042204.Peer-Reviewed Original ResearchConceptsRegulation of protein-protein interactionsProtein-protein interactionsNon-lamellar lipidsMembrane hydrophobic coreMembrane remodelingMechanical properties of lipid bilayersMembrane bindingProperties of lipid bilayersRegulatory functionsTubulin bindingTubulinHydrophobic regionLipid headgroupsHydrophobic coreCell proliferationLipid bilayerPlanar lipid membranesMembrane mechanical propertiesMembraneMolecular probesLipid packingLipidLipid membranesGramicidin A channelBinding
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 distributionNanoporesMoleculesΑSynTraps
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
2015
Evidence of Distinct Channel Conformations for the Mitochondrial Outer Membrane Translocase Tom40
Kuszak A, Jacobs D, Gurnev P, Lithgow T, Bezrukov S, Rostovtseva T, Buchanan S. Evidence of Distinct Channel Conformations for the Mitochondrial Outer Membrane Translocase Tom40. The FASEB Journal 2015, 29 DOI: 10.1096/fasebj.29.1_supplement.777.7.Peer-Reviewed Original ResearchN- and C-terminiC-terminiTOM complexSubunit of mitochondrial ATP synthaseMitochondrial ATP synthaseSubstrate binding affinityPresequence peptideC. glabrataSubstrate recognitionMitochondrial proteinsTom40Mitochondrial membraneOuter membraneATP synthaseTruncated formStructural basisSubstrate processingPore-forming subunitConstriction zonePlanar lipid membranesBinding affinityFunctional locationLipid membranesMembranePresequence