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 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
2017
Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes
Hoogerheide D, Noskov S, Jacobs D, Bergdoll L, Silin V, Worcester D, Abramson J, Nanda H, Rostovtseva T, Bezrukov S. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e3622-e3631. PMID: 28420794, PMCID: PMC5422764, DOI: 10.1073/pnas.1619806114.Peer-Reviewed Original ResearchConceptsMitochondrial outer membraneMitochondrial membraneOuter membraneDimeric tubulinPeripheral membrane proteinsMembrane-binding domainOuter mitochondrial membraneDomain of tubulinIntegral proteinsMembrane proteinsCytosolic proteinsPhysiological roleHelix H10TubulinLipid headgroupsProteinComplex mechanismsMembranePeripheral bindingStructural featuresEssential stepCytoskeletonElectrochemical impedance spectroscopyMitochondriaDomain
2015
Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40*
Kuszak A, Jacobs D, Gurnev P, Shiota T, Louis J, Lithgow T, Bezrukov S, Rostovtseva T, Buchanan S. Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40*. Journal Of Biological Chemistry 2015, 290: 26204-26217. PMID: 26336107, PMCID: PMC4646270, DOI: 10.1074/jbc.m115.642173.Peer-Reviewed Original ResearchConceptsC-terminal domainPresequence peptideC-terminusMitochondrial outer membraneAmino acidsΒ-barrel domainYeast Candida glabrataOuter membrane complexSubstrate Binding AffinityTranslocase complexNuclear genomeTom40 proteinMitochondrial proteinsProtein transportTom40Substrate recognitionHelical domainOuter membraneMembrane complexCentral subunitN-terminusPlanar lipid membranesTransport functionTerminusChannel conformationEvidence 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