2023
Turbocharging synaptic transmission
Rothman J, Grushin K, Bera M, Pincet F. Turbocharging synaptic transmission. FEBS Letters 2023, 597: 2233-2249. PMID: 37643878, DOI: 10.1002/1873-3468.14718.Peer-Reviewed Original Research
2022
The beginning and the end of SNARE‐induced membrane fusion
Mion D, Bunel L, Heo P, Pincet F. The beginning and the end of SNARE‐induced membrane fusion. FEBS Open Bio 2022, 12: 1958-1979. PMID: 35622519, PMCID: PMC9623537, DOI: 10.1002/2211-5463.13447.Peer-Reviewed Original Research
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
2016
A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion
Xu W, Nathwani B, Lin C, Wang J, Karatekin E, Pincet F, Shih W, Rothman JE. A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion. Journal Of The American Chemical Society 2016, 138: 4439-4447. PMID: 26938705, PMCID: PMC4950518, DOI: 10.1021/jacs.5b13107.Peer-Reviewed Original ResearchConceptsMembrane fusionSoluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexCore molecular machineryMembrane fusion eventsProtein receptor complexMembrane fusion processMolecular machineryDNA origami platformTarget membraneAuxiliary proteinsIntracellular communicationDocking stepSingle-event levelReceptor complexLipid mixingSmall unilamellar vesiclesLipid bilayersSnareFundamental processesVesiclesUnilamellar vesiclesTraffickingMachineryProteinFusion
2015
Accelerating SNARE‐Mediated Membrane Fusion by DNA–Lipid Tethers
Xu W, Wang J, Rothman J, Pincet F. Accelerating SNARE‐Mediated Membrane Fusion by DNA–Lipid Tethers. Angewandte Chemie 2015, 127: 14596-14600. DOI: 10.1002/ange.201506844.Peer-Reviewed Original ResearchDNA-lipidMembrane-distal endMembrane-proximal endArtificial tetherSNARE functionCore machinerySNARE proteinsProtein functionTarget membraneMembrane fusionBiological processesNative proteinBase pairsLipid mixingMaximum fusion rateProgrammable toolsBase-pair hybridizationProteinSnareMembraneFusionMachineryTetherNucleotidesVesicles
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 stagesZippering
2011
Complexin cross-links prefusion SNAREs into a zigzag array
Kümmel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM. Complexin cross-links prefusion SNAREs into a zigzag array. Nature Structural & Molecular Biology 2011, 18: 927-933. PMID: 21785414, PMCID: PMC3410656, DOI: 10.1038/nsmb.2101.Peer-Reviewed Original Research
2008
The Surface Force Apparatus to Reveal the Energetics of Biomolecules Assembly. Application to DNA Bases Pairing and SNARE Fusion Proteins Folding
Perez E, Li F, Tareste D, Pincet F. The Surface Force Apparatus to Reveal the Energetics of Biomolecules Assembly. Application to DNA Bases Pairing and SNARE Fusion Proteins Folding. Cellular And Molecular Bioengineering 2008, 1: 240. DOI: 10.1007/s12195-008-0025-7.Peer-Reviewed Original ResearchSNARE proteinsLipid bilayersMolecular binding energyIntracellular fusion eventsSurface force apparatusIntermediate assembly statesSNAREpin assemblyNanoscale resolutionBiomolecule assemblyForce apparatusSFA measurementsBiological moleculesBinding energiesLipid headgroupsFusion eventsMembrane fusionFusion proteinInteraction energyConformational changesAssembly stateAdhesion forceDNA basesProteinBilayersEnergy
2004
Hemifusion and fusion of giant vesicles induced by reduction of inter-membrane distance
Heuvingh J, Pincet F, Cribier S. Hemifusion and fusion of giant vesicles induced by reduction of inter-membrane distance. The European Physical Journal E 2004, 14: 269-276. PMID: 15338438, DOI: 10.1140/epje/i2003-10151-2.Peer-Reviewed Original ResearchConceptsInter-membrane distanceGiant unilamellar vesiclesInner leafletMembrane fusionOuter leafletMeans of micromanipulationCommon functionFluorescence microscopyProbe redistributionVesiclesInfluenza virus hemagglutininGiant vesiclesDNA basesModel systemHemifusionUnilamellar vesiclesActual fusionVirus hemagglutininMembraneContact zoneFusionHead groupsGood agreementProteinLeaflets