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
2022
The Get1/2 insertase forms a channel to mediate the insertion of tail-anchored proteins into the ER
Heo P, Culver J, Miao J, Pincet F, Mariappan M. The Get1/2 insertase forms a channel to mediate the insertion of tail-anchored proteins into the ER. Cell Reports 2022, 42: 111921. PMID: 36640319, PMCID: PMC9932932, DOI: 10.1016/j.celrep.2022.111921.Peer-Reviewed Original ResearchConceptsTransmembrane domainTA proteinsSingle C-terminal transmembrane domainC-terminal transmembrane domainTail-anchored (TA) proteinsTail-anchored proteinsEndoplasmic reticulum membraneGet3Reticulum membraneChannel functionInsertaseBulk fluorescenceAqueous channelsProteinChannel activityMutation analysisMembraneMicrofluidic assayTranslocaseYeastComplexesInsertionTranslocationHydrophilic segmentsBinding
2020
CX3CL1 homo-oligomerization drives cell-to-cell adherence
Ostuni M, Hermand P, Saindoy E, Guillou N, Guellec J, Coens A, Hattab C, Desuzinges-Mandon E, Jawhari A, Iatmanen-Harbi S, Lequin O, Fuchs P, Lacapere J, Combadière C, Pincet F, Deterre P. CX3CL1 homo-oligomerization drives cell-to-cell adherence. Scientific Reports 2020, 10: 9069. PMID: 32494000, PMCID: PMC7271195, DOI: 10.1038/s41598-020-65988-w.Peer-Reviewed Original ResearchConceptsNumerous adhesion moleculesPhotobleaching assaysNative electrophoresisAdhesive potencyTransmembrane peptidesLipid environmentKey immune processesAdhesive functionFluorescence recoveryFunctional roleDomain peptideFluorescence kineticsOligomerizationCellular adherenceMolecular modelingAdhesion moleculesCell adherenceTransmembrane chemokineImmune processesCompact bundlePeptidesBlood leukocytesClustersElectrophoresisCX3CL1TANGO1 membrane helices create a lipid diffusion barrier at curved membranes
Raote I, Ernst AM, Campelo F, Rothman JE, Pincet F, Malhotra V. TANGO1 membrane helices create a lipid diffusion barrier at curved membranes. ELife 2020, 9: e57822. PMID: 32452385, PMCID: PMC7266638, DOI: 10.7554/elife.57822.Peer-Reviewed Original Research
2016
Endothelial basement membrane laminin 511 is essential for shear stress response
Di Russo J, Luik A, Yousif L, Budny S, Oberleithner H, Hofschröer V, Klingauf J, van Bavel E, Bakker E, Hellstrand P, Bhattachariya A, Albinsson S, Pincet F, Hallmann R, Sorokin L. Endothelial basement membrane laminin 511 is essential for shear stress response. The EMBO Journal 2016, 36: 183-201. PMID: 27940654, PMCID: PMC5239996, DOI: 10.15252/embj.201694756.Peer-Reviewed Original ResearchConceptsCell-cell adhesion strengthLaminin-511Junctional complexesVE-cadherinIntegrin-mediated interactionsEndothelial basement membrane componentVinculin-positive focal adhesionsCatenin associationFocal adhesionsStress responseCell junctionsMembrane componentsBasement membrane componentsBasement membraneArterial endotheliumCortical stiffnessMechanotransductionPECAM-1Firm anchorageEndothelial basement membraneJunctional associationMembraneConsiderable informationComplexesAdhesionOn-Chip Quantitative Measurement of Mechanical Stresses During Cell Migration with Emulsion Droplets
Molino D, Quignard S, Gruget C, Pincet F, Chen Y, Piel M, Fattaccioli J. On-Chip Quantitative Measurement of Mechanical Stresses During Cell Migration with Emulsion Droplets. Scientific Reports 2016, 6: 29113. PMID: 27373558, PMCID: PMC4931467, DOI: 10.1038/srep29113.Peer-Reviewed Original Research
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 eggsGametesMachineryAdhesionSpeciesProteinCalcium 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 ResearchConceptsSynaptic 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 arrangementArf1/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
COPI buds 60-nm lipid droplets from reconstituted water–phospholipid–triacylglyceride interfaces, suggesting a tension clamp function
Thiam AR, Antonny B, Wang J, Delacotte J, Wilfling F, Walther TC, Beck R, Rothman JE, Pincet F. COPI buds 60-nm lipid droplets from reconstituted water–phospholipid–triacylglyceride interfaces, suggesting a tension clamp function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 13244-13249. PMID: 23901109, PMCID: PMC3746913, DOI: 10.1073/pnas.1307685110.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation Factor 1AnimalsCoat Protein Complex IEscherichia coliHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMicroscopy, ElectronPhosphatidylcholinesPhosphatidylethanolaminesPhospholipidsProtein TransportSf9 CellsSpectrometry, FluorescenceSpodopteraSurface TensionTransport VesiclesTriglyceridesWaterConceptsCoat protein complex ILipid dropletsCoat protein complexTransport vesicle formationProtein complex ILipid droplet targetingBud vesiclesCOPI subunitsProtein complexesCoat componentsNeighboring proteinsIntracellular traffickingVesicle formationComplex IClamp functionPossible direct interactionDirect interactionPhospholipid packingUnsuitable targetsProteinBilayer membranesCoatomerMembraneOrganellesProtomers
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 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 2Complexin 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
2010
Recent Applications of Fluorescence Recovery after Photobleaching (FRAP) to Membrane Bio-Macromolecules
Rayan G, Guet J, Taulier N, Pincet F, Urbach W. Recent Applications of Fluorescence Recovery after Photobleaching (FRAP) to Membrane Bio-Macromolecules. Sensors 2010, 10: 5927-5948. PMID: 22219695, PMCID: PMC3247740, DOI: 10.3390/s100605927.Peer-Reviewed Original ResearchThe adhesion mediated by the P-selectin P–selectin glycoprotein ligand-1 (PSGL-1) couple is stronger for shorter PSGL-1 variants
Barbaux S, Poirier O, Pincet F, Hermand P, Tiret L, Deterre P. The adhesion mediated by the P-selectin P–selectin glycoprotein ligand-1 (PSGL-1) couple is stronger for shorter PSGL-1 variants. Journal Of Leukocyte Biology 2010, 87: 727-734. PMID: 20051472, DOI: 10.1189/jlb.0609408.Peer-Reviewed Original Research
2008
Functional Adhesiveness of the CX3CL1 Chemokine Requires Its Aggregation ROLE OF THE TRANSMEMBRANE DOMAIN*
Hermand P, Pincet F, Carvalho S, Ansanay H, Trinquet E, Daoudi M, Combadière C, Deterre P. Functional Adhesiveness of the CX3CL1 Chemokine Requires Its Aggregation ROLE OF THE TRANSMEMBRANE DOMAIN*. Journal Of Biological Chemistry 2008, 283: 30225-30234. PMID: 18725411, PMCID: PMC2662081, DOI: 10.1074/jbc.m802638200.Peer-Reviewed Original ResearchConceptsBioluminescence resonance energy transferHomogeneous time-resolved fluorescenceTransmembrane domainAdhesive potencyTransmembrane domain residuesLoss of glycosylationConstitutive oligomersDomain residuesBRET signalTruncation experimentsResonance energy transferCell surfacePrimary cellsSpecific signalsNative formAdhesion assaysAdhesive moleculesCell linesCentral roleAggregation roleInhibition of CX3CL1New pathwayTime-resolved fluorescenceCellsAssays
2004
Separation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3*
Martinez-Rico C, Pincet F, Perez E, Thiery J, Shimizu K, Takai Y, Dufour S. Separation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3*. Journal Of Biological Chemistry 2004, 280: 4753-4760. PMID: 15550395, DOI: 10.1074/jbc.m412544200.Peer-Reviewed Original ResearchConceptsE-cadherin-based adhesionsNectin-3E-cadherin-dependent cell adhesionExtracellular fragmentE-cadherin-mediated adhesionE-cadherin-expressing cellsNectin-1Cell adhesionCell-cell adhesionIndependent cell adhesion moleculesAdherens junctionsCell adhesion moleculeCell doubletsSignificant agonistic effectKey moleculesE-cadherinL cellsCadherinNectinAdhesion moleculesCellsAdhesionFragmentsHomodimerHeterodimersSpecific Recognition of Macroscopic Objects by the Cell Surface: Evidence for a Receptor Density Threshold Revealed by Micrometric Particle Binding Characteristics
Sarda S, Pointu D, Pincet F, Henry N. Specific Recognition of Macroscopic Objects by the Cell Surface: Evidence for a Receptor Density Threshold Revealed by Micrometric Particle Binding Characteristics. Biophysical Journal 2004, 86: 3291-3303. PMID: 15111442, PMCID: PMC1304194, DOI: 10.1016/s0006-3495(04)74377-5.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CD19Binding SitesBiophysicsBiotinylationCell AdhesionCell Line, TransformedCell Line, TumorCell MembraneDiffusionFlow CytometryHumansKineticsLigandsLymphoma, B-CellMicroscopy, FluorescenceModels, BiologicalProtein BindingScattering, RadiationStreptavidinStress, MechanicalSurface PropertiesTemperatureTime FactorsEnhanced Adhesive Capacities of the Naturally Occurring Ile249–Met280 Variant of the Chemokine Receptor CX3CR1*
Daoudi M, Lavergne E, Garin A, Tarantino N, Debré P, Pincet F, Combadière C, Deterre P. Enhanced Adhesive Capacities of the Naturally Occurring Ile249–Met280 Variant of the Chemokine Receptor CX3CR1*. Journal Of Biological Chemistry 2004, 279: 19649-19657. PMID: 14990582, DOI: 10.1074/jbc.m313457200.Peer-Reviewed Original Research