2024
Quantitative single-molecule analysis of assembly and Ca2+-dependent disassembly of synaptotagmin oligomers on lipid bilayers
Li F, Coleman J, Redondo-Morata L, Kalyana Sundaram R, Stroeva E, Rothman J, Pincet F. Quantitative single-molecule analysis of assembly and Ca2+-dependent disassembly of synaptotagmin oligomers on lipid bilayers. Communications Biology 2024, 7: 1608. PMID: 39627539, PMCID: PMC11615320, DOI: 10.1038/s42003-024-07317-9.Peer-Reviewed Original ResearchConceptsSyt-1Lipid bilayerRing-like oligomersCa2+-evoked releaseSynaptotagmin-1Single-molecule imaging methodsSynaptic vesiclesBiochemical evidencePhysiological requirementsOligomerizationAnalysis of assembliesBilayerOligomersCa2+LipidAssemblyCa2Classes of oligomersMutationsVesiclesDisassemblyEvoked release
2018
Rearrangements under confinement lead to increased binding energy of Synaptotagmin‐1 with anionic membranes in Mg2+ and Ca2+
Gruget C, Coleman J, Bello O, Krishnakumar SS, Perez E, Rothman JE, Pincet F, Donaldson SH. Rearrangements under confinement lead to increased binding energy of Synaptotagmin‐1 with anionic membranes in Mg2+ and Ca2+. FEBS Letters 2018, 592: 1497-1506. PMID: 29578584, DOI: 10.1002/1873-3468.13040.Peer-Reviewed Original Research
2014
Calcium 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
2012
SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open
Shi L, Shen QT, Kiel A, Wang J, Wang HW, Melia TJ, Rothman JE, Pincet F. SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open. Science 2012, 335: 1355-1359. PMID: 22422984, PMCID: PMC3736847, DOI: 10.1126/science.1214984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumDiffusionLipid BilayersLiposomesMembrane FusionMembrane ProteinsMiceNeurotransmitter AgentsProtein Structure, TertiaryProteolipidsRatsRecombinant Fusion ProteinsSNARE ProteinsSynaptic TransmissionSynaptic VesiclesSynaptosomal-Associated Protein 25Syntaxin 1Vesicle-Associated Membrane Protein 2ConceptsVesicle-associated membrane protein 2Bilayer fusionNative transmembrane domainNascent fusion poresLipid bilayer nanodiscsMembrane protein 2Synchronous neurotransmitter releaseSNARE complexTransmembrane helicesTransmembrane domainBilayer nanodiscsFused bilayersFusion porePore opensFusion partnerBiochemical studiesProtein 2Neurotransmitter releaseNanodiscsSnareEfficient releaseSynaptic transmissionSNAREpinsFusionRelevant time scales
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 and non specific interactions involving LeX determinant quantified by lipid vesicle micromanipulation
Gourier C, Pincet F, Perez E, Zhang Y, Mallet J, Sinaÿ P. Specific and non specific interactions involving LeX determinant quantified by lipid vesicle micromanipulation. Glycoconjugate Journal 2004, 21: 165-174. PMID: 15483381, DOI: 10.1023/b:glyc.0000044847.15797.2e.Peer-Reviewed Original ResearchEnhanced 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
2001
Ultraweak Sugar-Sugar Interactions for Transient Cell Adhesion
Pincet F, Le Bouar T, Zhang Y, Esnault J, Mallet J, Perez E, Sinaÿ P. Ultraweak Sugar-Sugar Interactions for Transient Cell Adhesion. Biophysical Journal 2001, 80: 1354-1358. PMID: 11222296, PMCID: PMC1301327, DOI: 10.1016/s0006-3495(01)76108-5.Peer-Reviewed Original Research