2024
Kinetic study of membrane protein interactions: from three to two dimensions
Adrien V, Reffay M, Taulier N, Verchère A, Monlezun L, Picard M, Ducruix A, Broutin I, Pincet F, Urbach W. Kinetic study of membrane protein interactions: from three to two dimensions. Scientific Reports 2024, 14: 882. PMID: 38195620, PMCID: PMC10776792, DOI: 10.1038/s41598-023-50827-5.Peer-Reviewed Original ResearchConceptsMembrane proteinsMembrane protein interactionsProtein-protein interactionsProtein complexesProtein interactionsMembrane environmentOpposite membranesBacterial efflux pumpsProtein behaviorProtein systemsMolecular interactionsEfflux pumpsProteinExploration distanceMembraneFluorescence recovery experimentsInteractionBinding rateBinding constantsComplexes
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 actionProteinAssemblyChaperonesSynaptotagminExocytosisBilayersDirect determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer
Panda A, Giska F, Duncan A, Welch A, Brown C, McAllister R, Hariharan P, Goder J, Coleman J, Ramakrishnan S, Pincet F, Guan L, Krishnakumar S, Rothman J, Gupta K. Direct determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer. Nature Methods 2023, 20: 891-897. PMID: 37106230, PMCID: PMC10932606, DOI: 10.1038/s41592-023-01864-5.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsOligomeric organizationOligomeric stateNative mass spectrometry analysisFunctional oligomeric stateKey membrane componentMass spectrometry analysisNMS analysisTarget membraneLipid bindingMembrane componentsProteolipid vesiclesMembrane compositionLipid compositionSpectrometry analysisLipid membranesNeurotransmitter releaseProteinMembraneLipidsMembrane propertiesDirect determinationBilayersTransporters
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 eggsGametesMachineryAdhesionSpeciesProtein
2011
CD9 tetraspanin generates fusion competent sites on the egg membrane for mammalian fertilization
Jégou A, Ziyyat A, Barraud-Lange V, Perez E, Wolf J, Pincet F, Gourier C. CD9 tetraspanin generates fusion competent sites on the egg membrane for mammalian fertilization. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 10946-10951. PMID: 21690351, PMCID: PMC3131345, DOI: 10.1073/pnas.1017400108.Peer-Reviewed Original ResearchConceptsAdhesion sitesFusion-competent sitesWild-type eggsCD9 tetraspaninEgg membrane proteinsSperm-egg fusionMembrane proteinsGamete membranesMammalian fertilizationCompetent sitesGamete interactionAdhesion eventsTight proximityEgg membraneCD9TetraspaninsEggsFertilizationMembraneStrong-interaction modesAdhesion probabilitySitesFusionInteraction modesProtein
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 Research