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 distributionNanoporesMoleculesΑSynTrapsA 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