2018
Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly
Ma L, Jiao J, Zhang Y. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly. Methods In Molecular Biology 2018, 1860: 95-114. PMID: 30317500, PMCID: PMC6441361, DOI: 10.1007/978-1-4939-8760-3_6.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE assemblyHigh-resolution optical tweezersN-ethylmaleimide-sensitive factor attachment protein receptorsMembrane fusionFactor attachment protein receptorsOptical tweezers studiesNeuronal SNARE assemblyIntracellular membrane fusionAttachment protein receptorsOptical tweezersΑ-SNAPDetailed experimental protocolCellular compartmentsRegulatory proteinsProtein receptorsDifferent cellsSpatiotemporal resolutionProteinAssemblyFusion processManipulation approachTweezersExperimental approachFusion
2017
Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers
Zhang Y. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers. Protein Science 2017, 26: 1252-1265. PMID: 28097727, PMCID: PMC5477538, DOI: 10.1002/pro.3116.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorSNARE assemblyMembrane fusionSNARE complexN-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsFast calcium-triggered fusionAttachment protein receptorsHigh-resolution optical tweezersCalcium-triggered fusionC-terminal domainFour-helix bundleNeurotransmitter-containing vesiclesLinker domainPlasma membraneDomain associationProtein receptorsMolecular engineDifferent functionsPathwayAssemblyMembraneOptical tweezersSynaptic transmission
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 receptorsZipperingα-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle
Ma L, Kang Y, Jiao J, Rebane AA, Cha HK, Xi Z, Qu H, Zhang Y. α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle. Cell Reports 2016, 15: 531-539. PMID: 27068468, PMCID: PMC4838522, DOI: 10.1016/j.celrep.2016.03.050.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsC-terminal domainN-terminal domainMembrane fusionLinker domainΑ-SNAPSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorN-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsIntracellular membrane fusionAttachment protein receptorsConformational selection mechanismFour-helix bundleSNARE assemblySNARE complexProtein receptorsDynamic assemblyStepwise assemblyAssemblyDomainFusionZipperingOptical tweezersRecent experimentsReceptors
2014
Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins
Zorman S, Rebane AA, Ma L, Yang G, Molski MA, Coleman J, Pincet F, Rothman JE, Zhang Y. Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins. ELife 2014, 3: e03348. PMID: 25180101, PMCID: PMC4166003, DOI: 10.7554/elife.03348.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsEnergy TransferHumansKineticsModels, MolecularMolecular Sequence DataMultiprotein ComplexesOptical TweezersProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondaryQa-SNARE ProteinsRatsSequence Homology, Amino AcidSNARE ProteinsThermodynamicsVesicle-Associated Membrane Protein 2Vesicular Transport ProteinsConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE complexN-ethylmaleimide-sensitive factor attachment protein receptorsMembrane fusionFactor attachment protein receptorsAttachment protein receptorsHigh-resolution optical tweezersNeuronal SNARE complexFolding/assemblyEnergy releaseSNARE proteinsSingle-molecule levelProtein receptorsDomain associationOptical tweezersTerminal partZippering mechanismFusion kineticsZipperingComplexesAssemblyDifferent energeticsEnergyYeastTweezers