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
2015
Phosphorylation of Complexin by PKA Regulates Activity-Dependent Spontaneous Neurotransmitter Release and Structural Synaptic Plasticity
Cho RW, Buhl LK, Volfson D, Tran A, Li F, Akbergenova Y, Littleton JT. Phosphorylation of Complexin by PKA Regulates Activity-Dependent Spontaneous Neurotransmitter Release and Structural Synaptic Plasticity. Neuron 2015, 88: 749-761. PMID: 26590346, PMCID: PMC4847943, DOI: 10.1016/j.neuron.2015.10.011.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAnimalsBase SequenceCalciumCyclic AMP-Dependent Protein KinasesDrosophilaDrosophila ProteinsExocytosisMolecular Sequence DataNerve Tissue ProteinsNeuromuscular JunctionNeuronal PlasticityNeurotransmitter AgentsPhosphorylationSNARE ProteinsSynaptic TransmissionConceptsSpontaneous neurotransmitter releaseActivity-dependent synaptic growthNeurotransmitter releasePKA-dependent phosphorylationActivity-dependent phosphorylationSynaptic plasticityPresynaptic release machinerySNARE complexRegulated traffickingActivity-dependent mannerC-terminusSynaptic growthSpontaneous releaseStructural synaptic plasticityPhosphorylationStructural plasticityRelease machineryPostsynaptic glutamate receptorsPlasticityNeuronal plasticityGlutamate receptorsSynaptic transmissionNervous systemKey roleFusion mechanism
2014
Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo
Cho RW, Kümmel D, Li F, Baguley SW, Coleman J, Rothman JE, Littleton JT. Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 10317-10322. PMID: 24982161, PMCID: PMC4104896, DOI: 10.1073/pnas.1409311111.Peer-Reviewed Original ResearchConceptsSNARE complexSpontaneous synaptic vesicle fusionSingle SNARE complexSNARE fusion machinerySynaptic vesicle fusionGenetic rescue approachStructure-function studiesDistinct molecular mechanismsVivo genetic manipulationCpx proteinsFusion clampTrans-SNAREFusion machineryTrans interactionsConformational switchGenetic manipulationGenetic analysisVesicle fusionMolecular mechanismsVesicle releaseRescue approachMutantsProteinSnareAdditional mechanism