2016
Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex
Zhang X, Rebane AA, Ma L, Li F, Jiao J, Qu H, Pincet F, Rothman JE, Zhang Y. Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e8031-e8040. PMID: 27911771, PMCID: PMC5167175, DOI: 10.1073/pnas.1605748113.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsMembrane FusionMiceMicroscopy, Atomic ForceMolecular Dynamics SimulationMunc18 ProteinsOptical TweezersProtein ConformationProtein DomainsProtein FoldingProtein StabilityQa-SNARE ProteinsSNARE ProteinsSynaptic TransmissionSynaptosomal-Associated Protein 25Vesicle-Associated Membrane Protein 2ConceptsSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorT-SNARE complexC-terminal domainN-terminal domainSNARE zipperingPlasma membraneN-ethylmaleimide-sensitive factor attachment protein receptorsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsTarget plasma membraneAttachment protein receptorsFour-helix bundleThree-helix bundleSynaptic vesicle fusionSingle-molecule force spectroscopyV-SNARESNARE assemblySNARE complexHelical bundleConformational switchC-terminusMembrane fusionVesicle fusionProtein receptorsZipperingKinetic barriers to SNAREpin assembly in the regulation of membrane docking/priming and fusion
Li F, Tiwari N, Rothman JE, Pincet F. Kinetic barriers to SNAREpin assembly in the regulation of membrane docking/priming and fusion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 10536-10541. PMID: 27601655, PMCID: PMC5035884, DOI: 10.1073/pnas.1604000113.Peer-Reviewed Original Research
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 mechanismRe-visiting the trans insertion model for complexin clamping
Krishnakumar SS, Li F, Coleman J, Schauder CM, Kümmel D, Pincet F, Rothman JE, Reinisch KM. Re-visiting the trans insertion model for complexin clamping. ELife 2015, 4: e04463. PMID: 25831964, PMCID: PMC4384536, DOI: 10.7554/elife.04463.Peer-Reviewed Original ResearchAdaptor Proteins, Vesicular TransportAlgorithmsAnimalsCalorimetryCircular DichroismEntropyFluorescence Resonance Energy TransferHumansKineticsMembrane FusionModels, NeurologicalMutationNerve Tissue ProteinsNeuronsProtein BindingSignal TransductionSNARE ProteinsSynaptic TransmissionSynaptotagminsVesicle-Associated Membrane Protein 2