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
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 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