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
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