2018
High-Throughput Monitoring of Single Vesicle Fusion Using Freestanding Membranes and Automated Analysis
Ramakrishnan S, Gohlke A, Li F, Coleman J, Xu W, Rothman JE, Pincet F. High-Throughput Monitoring of Single Vesicle Fusion Using Freestanding Membranes and Automated Analysis. Langmuir 2018, 34: 5849-5859. PMID: 29694054, DOI: 10.1021/acs.langmuir.8b00116.Peer-Reviewed Original ResearchConceptsMembrane fusionFusion eventsSoluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteinsSNARE-dependent membrane fusionIndividual vesicle fusion eventsFactor attachment protein receptor proteinsN-ethylmaleimide-sensitive factor attachment protein receptor proteinsT-SNARE proteinsSingle-vesicle fusionProtein receptor proteinsVesicle fusion eventsMobility of proteinsVesicle dockingContent releaseVesicle fusionHigh-throughput monitoringPlanar membranesReceptor proteinLipid mixingProteinLipid bilayersVesiclesCorrect reconstitutionMembraneAqueous compartment
2017
Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly
Rebane AA, Wang B, Ma L, Qu H, Coleman J, Krishnakumar S, Rothman JE, Zhang Y. Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly. Journal Of Molecular Biology 2017, 430: 479-490. PMID: 29056461, PMCID: PMC5805579, DOI: 10.1016/j.jmb.2017.10.012.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment receptorSNARE assemblySynaptic exocytosisMembrane fusionSingle-molecule optical tweezersT-SNARE complexVesicle-associated SNAREsTarget plasma membraneC-terminal assemblyFour-helix bundleC-terminal regionSNARE complexPlasma membraneMolecular mechanismsZipperingMutationsNumerous diseasesAssembly energyNeurotransmitter releaseExocytosisAttachment receptorAssemblyNeurological disordersOptical tweezersComplexes
2014
A Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion
Li F, Kümmel D, Coleman J, Reinisch KM, Rothman JE, Pincet F. A Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion. Journal Of The American Chemical Society 2014, 136: 3456-3464. PMID: 24533674, PMCID: PMC3985920, DOI: 10.1021/ja410690m.Peer-Reviewed Original ResearchConceptsN-terminal domainMembrane fusionV-SNARET-SNAREsRecent biophysical studiesC-terminal portionSNARE complexTransmembrane domainRegulatory proteinsFunctional intermediatesC-terminusDistinct functionsN-terminusMolecular mechanismsConformational rearrangementsBiophysical studiesVital regulatorZippering mechanismRate-limiting stepBiological membranesSnareFusionComplexinMultiple stagesZipperingCommon intermediates and kinetics, but different energetics, in the assembly of SNARE proteins
Zorman S, Rebane AA, Ma L, Yang G, Molski MA, Coleman J, Pincet F, Rothman JE, Zhang Y. Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins. ELife 2014, 3: e03348. PMID: 25180101, PMCID: PMC4166003, DOI: 10.7554/elife.03348.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsEnergy TransferHumansKineticsModels, MolecularMolecular Sequence DataMultiprotein ComplexesOptical TweezersProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondaryQa-SNARE ProteinsRatsSequence Homology, Amino AcidSNARE ProteinsThermodynamicsVesicle-Associated Membrane Protein 2Vesicular Transport ProteinsConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE complexN-ethylmaleimide-sensitive factor attachment protein receptorsMembrane fusionFactor attachment protein receptorsAttachment protein receptorsHigh-resolution optical tweezersNeuronal SNARE complexFolding/assemblyEnergy releaseSNARE proteinsSingle-molecule levelProtein receptorsDomain associationOptical tweezersTerminal partZippering mechanismFusion kineticsZipperingComplexesAssemblyDifferent energeticsEnergyYeastTweezers
2011
Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex
Shi L, Kümmel D, Coleman J, Melia TJ, Giraudo CG. Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex. Molecular Biology Of The Cell 2011, 22: 4150-4160. PMID: 21900493, PMCID: PMC3204075, DOI: 10.1091/mbc.e11-02-0150.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalorimetryCell MembraneHeLa CellsHuman Growth HormoneHumansLiposomesMiceMicroscopy, FluorescenceMolecular ChaperonesMunc18 ProteinsNeuroendocrine CellsPC12 CellsProtein BindingProtein Interaction Domains and MotifsProtein TransportRatsRecombinant ProteinsSNARE ProteinsSyntaxin 1ThermodynamicsTitrimetryConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSyntaxin 1AMunc18-1N-ethylmaleimide-sensitive factor attachment protein receptorsSec1/Munc18 (SM) proteinsFactor attachment protein receptorsCentral cavitySNARE complex assemblyIntracellular membrane traffickingAttachment protein receptorsMunc18-1 mutantsLiposome fusionPrecise molecular mechanismsMunc18 proteinsMembrane traffickingSNARE complexChaperone functionH3 domainDistinct binding modesMembrane fusionMolecular mechanismsProtein receptorsDual functionNeuroendocrine cellsBinding modes