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
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
Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 accumulation in the intercellular contact area prior to fusion during mammalian fertilization
Chalbi M, Barraud-Lange V, Ravaux B, Howan K, Rodriguez N, Soule P, Ndzoudi A, Boucheix C, Rubinstein E, Wolf J, Ziyyat A, Perez E, Pincet F, Gourier C. Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 accumulation in the intercellular contact area prior to fusion during mammalian fertilization. Development 2014, 141: 3732-3739. PMID: 25209248, DOI: 10.1242/dev.111534.Peer-Reviewed Original ResearchConceptsGamete fusionMammalian fertilizationMolecular mechanismsSperm protein IZUMO1Intercellular contact areaFusion machineryMembrane proteinsMembrane organizationIZUMO1Intercellular adhesionAdhesion partnersRecruitment kineticsKey playersCD9Adhesion phaseEggsAdhesion areaFertilizationFusionHuman eggsGametesMachineryAdhesionSpeciesProteinArf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting
Wilfling F, Thiam AR, Olarte MJ, Wang J, Beck R, Gould TJ, Allgeyer ES, Pincet F, Bewersdorf J, Farese RV, Walther TC. Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. ELife 2014, 3: e01607. PMID: 24497546, PMCID: PMC3913038, DOI: 10.7554/elife.01607.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation Factor 1AnimalsBiological TransportCell LineCoat Protein Complex ICOP-Coated VesiclesDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumHumansLipaseLipid DropletsLipolysisMiceNanoparticlesParticle SizePhospholipidsRNA InterferenceSurface TensionTime FactorsTransfectionTriglyceridesConceptsCellular lipid dropletsLipid dropletsProtein machineryProtein targetingUbiquitous organellesVesicle traffickingLD surfaceSpecific proteinsKey enzymeLD morphologyMembrane precursorsMachineryMetabolic energyProteinNeutral lipidsTG storageEnzymeUnclear mechanismsAmount of phospholipidsRecent evidenceOrganellesCOPITraffickingTriacylglycerolsBuds
2013
Preparation and characterization of SNARE-containing nanodiscs and direct study of cargo release through fusion pores
Shi L, Howan K, Shen QT, Wang YJ, Rothman JE, Pincet F. Preparation and characterization of SNARE-containing nanodiscs and direct study of cargo release through fusion pores. Nature Protocols 2013, 8: 935-948. PMID: 23598444, DOI: 10.1038/nprot.2013.048.Peer-Reviewed Original ResearchConceptsFusion eventsScaffold proteinFusion poreMembrane scaffold proteinFluorescent lipidFluorescence-based approachFusion machineryAccessible lipidsCognate proteinNanodiscsPore expansionLipid bilayersProteinCargo releaseCargoLipidsPlate readerVAMP2MachineryFluorescenceSnareEncapsulated cargoDirect studyReleaseAssays