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 arrangement
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