2016
Snapshot of sequential SNARE assembling states between membranes shows that N-terminal transient assembly initializes fusion
Wang YJ, Li F, Rodriguez N, Lafosse X, Gourier C, Perez E, Pincet F. Snapshot of sequential SNARE assembling states between membranes shows that N-terminal transient assembly initializes fusion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 3533-3538. PMID: 26979957, PMCID: PMC4822643, DOI: 10.1073/pnas.1518935113.Peer-Reviewed Original ResearchConceptsFörster resonance energy transferProminent biological processesIntermembrane spaceSNARE proteinsTransmembrane complexTerminal domainInvolved proteinsBiological processesTransient assemblyResonance energy transferProteinSnareIntermembrane distanceMembraneAssemblyMolecular assembliesPathwayComplexes
2015
Formation of Giant Unilamellar Proteo-Liposomes by Osmotic Shock
Motta I, Gohlke A, Adrien V, Li F, Gardavot H, Rothman JE, Pincet F. Formation of Giant Unilamellar Proteo-Liposomes by Osmotic Shock. Langmuir 2015, 31: 7091-7099. PMID: 26038815, PMCID: PMC4950989, DOI: 10.1021/acs.langmuir.5b01173.Peer-Reviewed Original ResearchConceptsGiant unilamellar vesiclesLipid-anchored proteinsOsmotic shockTrans-membrane proteinsSingle giant unilamellar vesiclesProtein substratesPeripheral proteinsSpecific lipidsDifferent proteinsPhotobleaching experimentsFluorescence recoveryCell membraneProteinLarge vesiclesPhysiological conditionsModel systemUnilamellar vesiclesPhospholipid bilayersVesiclesSimple generic methodPrevious dataMembraneHigh concentrationsLipidsBilayers
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 ResearchMeSH KeywordsAnimalsCell MembraneKineticsMembrane FusionMiceModels, MolecularProtein Structure, TertiaryRatsSNARE ProteinsThermodynamicsConceptsN-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 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 ResearchComplexin 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 ResearchA conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion
Krishnakumar SS, Radoff DT, Kümmel D, Giraudo CG, Li F, Khandan L, Baguley SW, Coleman J, Reinisch KM, Pincet F, Rothman JE. A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion. Nature Structural & Molecular Biology 2011, 18: 934-940. PMID: 21785412, PMCID: PMC3668341, DOI: 10.1038/nsmb.2103.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayHumansMembrane FusionModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsProtein Structure, TertiaryRatsSynaptosomal-Associated Protein 25SynaptotagminsSyntaxin 1Vesicle-Associated Membrane Protein 2
2007
Confinement Free Energy of Surfaces Bearing End-Grafted Polymers in the Mushroom Regime and Local Measurement of the Polymer Density
Li F, Pincet F. Confinement Free Energy of Surfaces Bearing End-Grafted Polymers in the Mushroom Regime and Local Measurement of the Polymer Density. Langmuir 2007, 23: 12541-12548. PMID: 17988162, DOI: 10.1021/la7021374.Peer-Reviewed Original ResearchConceptsPolymer chainsMushroom regimeFree energyEnd-Grafted PolymersSurface force measurementsSingle polymer chainSurface force apparatusEnd-tethered polymer chainsInteraction free energyGrafted polymersForce apparatusPolymer densityForce profilesPolymersConfinement free energyPolymer theoryLipid bilayersIdentical surfacesMushroomlike structuresFree energy approximationForce measurementsSurfacePlanar surfaceGood precisionChain