2024
Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion
Caruel M, Pincet F. Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion. Biomolecules 2024, 14: 600. PMID: 38786007, PMCID: PMC11117985, DOI: 10.3390/biom14050600.Peer-Reviewed Original Research
2023
Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle
Bera M, Radhakrishnan A, Coleman J, Sundaram R, Ramakrishnan S, Pincet F, Rothman J. Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2311484120. PMID: 37903271, PMCID: PMC10636311, DOI: 10.1073/pnas.2311484120.Peer-Reviewed Original ResearchConceptsSpecific molecular functionsSynaptic vesicle protein synaptophysinTarget membrane bilayerSensor synaptotagminSNARE proteinsMolecular functionsMembrane proteinsSNAREpinsReceptor vesiclesSingle-molecule measurementsGene knockoutMembrane bilayerLipid bilayersProtein synaptophysinVesiclesDetergent extractsHexamer structureSYPMechanism of actionProteinAssemblyChaperonesSynaptotagminExocytosisBilayersDiacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles
Li F, Grushin K, Coleman J, Pincet F, Rothman J. Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2306086120. PMID: 37883433, PMCID: PMC10623011, DOI: 10.1073/pnas.2306086120.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
2019
SNARE machinery is optimized for ultrafast fusion
Manca F, Pincet F, Truskinovsky L, Rothman JE, Foret L, Caruel M. SNARE machinery is optimized for ultrafast fusion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 2435-2442. PMID: 30700546, PMCID: PMC6377469, DOI: 10.1073/pnas.1820394116.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 ResearchMeSH KeywordsDNADNA, Single-StrandedLipid BilayersLiposomesMembrane FusionProtein BindingSNARE ProteinsVesicular Transport ProteinsConceptsMembrane 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
2014
Calcium sensitive ring-like oligomers formed by synaptotagmin
Wang J, Bello O, Auclair SM, Wang J, Coleman J, Pincet F, Krishnakumar SS, Sindelar CV, Rothman JE. Calcium sensitive ring-like oligomers formed by synaptotagmin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 13966-13971. PMID: 25201968, PMCID: PMC4183308, DOI: 10.1073/pnas.1415849111.Peer-Reviewed Original ResearchMeSH KeywordsCalciumHumansLipid BilayersMultiprotein ComplexesProtein Structure, TertiarySNARE ProteinsSynaptotagmin IConceptsSynaptic vesicle protein Synaptotagmin 1Cytosolic domainSoluble N-ethylmaleimide-sensitive factorN-ethylmaleimide-sensitive factorMembrane fusion machineryReceptor complex assemblyRing-like oligomersFusion machineryC2 domainComplex assemblySynaptotagmin-1Helical reconstructionFusion proceedsNovel mechanismStructural mechanismsLipid monolayersNeurotransmitter releaseAbsence of calciumPhysiological concentrationsRing formationPresence of calciumFree calcium ionsSynaptotagminCalcium influxCircular arrangementA 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
2012
SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open
Shi L, Shen QT, Kiel A, Wang J, Wang HW, Melia TJ, Rothman JE, Pincet F. SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open. Science 2012, 335: 1355-1359. PMID: 22422984, PMCID: PMC3736847, DOI: 10.1126/science.1214984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumDiffusionLipid BilayersLiposomesMembrane FusionMembrane ProteinsMiceNeurotransmitter AgentsProtein Structure, TertiaryProteolipidsRatsRecombinant Fusion ProteinsSNARE ProteinsSynaptic TransmissionSynaptic VesiclesSynaptosomal-Associated Protein 25Syntaxin 1Vesicle-Associated Membrane Protein 2ConceptsVesicle-associated membrane protein 2Bilayer fusionNative transmembrane domainNascent fusion poresLipid bilayer nanodiscsMembrane protein 2Synchronous neurotransmitter releaseSNARE complexTransmembrane helicesTransmembrane domainBilayer nanodiscsFused bilayersFusion porePore opensFusion partnerBiochemical studiesProtein 2Neurotransmitter releaseNanodiscsSnareEfficient releaseSynaptic transmissionSNAREpinsFusionRelevant time scales
2011
Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state
Li F, Pincet F, Perez E, Giraudo CG, Tareste D, Rothman JE. Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state. Nature Structural & Molecular Biology 2011, 18: 941-946. PMID: 21785413, PMCID: PMC3736826, DOI: 10.1038/nsmb.2102.Peer-Reviewed Original Research
2007
Energetics and dynamics of SNAREpin folding across lipid bilayers
Li F, Pincet F, Perez E, Eng WS, Melia TJ, Rothman JE, Tareste D. Energetics and dynamics of SNAREpin folding across lipid bilayers. Nature Structural & Molecular Biology 2007, 14: 890-896. PMID: 17906638, DOI: 10.1038/nsmb1310.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsLipid BilayersMembrane FusionMiceProtein ConformationProtein FoldingRatsSNARE ProteinsSurface Properties