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
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
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 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