2025
Single-molecule two- and three-colour FRET studies reveal a transition state in SNARE disassembly by NSF
Cheppali S, Li C, Xing W, Sun R, Yang M, Xue Y, Lu S, Yao J, Sun S, Chen C, Sui S. Single-molecule two- and three-colour FRET studies reveal a transition state in SNARE disassembly by NSF. Nature Communications 2025, 16: 250. PMID: 39747074, PMCID: PMC11695992, DOI: 10.1038/s41467-024-55531-0.Peer-Reviewed Original ResearchConceptsN-ethylmaleimide sensitive factorSNARE complexDisassembly of SNARE complexesStable four-helix bundleFour-helix bundleSNARE motifFluorescence spectroscopy approachesMinimal machineryAAA+ ATPasesProtein machineryAdapter proteinVesicle fusionMembrane fusionSyntaxinPhysiological processesSnareProteinN-ethylmaleimideDisassemblySequential disassemblyMachinerySequential pathwayPathwayEukaryotesFusion
2022
A dynamic template complex mediates Munc18-chaperoned SNARE assembly
Yang J, Jin H, Liu Y, Guo Y, Zhang Y. A dynamic template complex mediates Munc18-chaperoned SNARE assembly. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2215124119. PMID: 36454760, PMCID: PMC9894263, DOI: 10.1073/pnas.2215124119.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE assemblyMunc18-3Munc18-1N-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsSNAP-25SNAP-25 bindingAttachment protein receptorsFour-helix bundleSynaptic vesicle fusionGlucose transporter translocationSNARE motifSNARE bundleSNAP-23Syntaxin 4GLUT4 translocationSyntaxin-1Transporter translocationPlasma membraneLinker regionMembrane fusionTemplate complexVesicle fusionMolecular mechanisms
2018
Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association
Jiao J, He M, Port SA, Baker RW, Xu Y, Qu H, Xiong Y, Wang Y, Jin H, Eisemann TJ, Hughson FM, Zhang Y. Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association. ELife 2018, 7: e41771. PMID: 30540253, PMCID: PMC6320071, DOI: 10.7554/elife.41771.Peer-Reviewed Original ResearchConceptsSNARE assemblyMunc18-1Sec1/Munc18-family (SM) proteinsSM protein Munc18-1Membrane fusionMunc18-1 mutationsNeuronal SNARE assemblyFour-helix bundleC-terminal regionN-terminal regionSingle-molecule force spectroscopySNARE motifSm proteinsSynaptic SNAREsMunc18-3SNARE zipperingProtein mechanismsTemplate complexForce spectroscopySnareZipperingProteinAssemblyComplexesVps33
2017
Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly
Rebane AA, Wang B, Ma L, Qu H, Coleman J, Krishnakumar S, Rothman JE, Zhang Y. Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly. Journal Of Molecular Biology 2017, 430: 479-490. PMID: 29056461, PMCID: PMC5805579, DOI: 10.1016/j.jmb.2017.10.012.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment receptorSNARE assemblySynaptic exocytosisMembrane fusionSingle-molecule optical tweezersT-SNARE complexVesicle-associated SNAREsTarget plasma membraneC-terminal assemblyFour-helix bundleC-terminal regionSNARE complexPlasma membraneMolecular mechanismsZipperingMutationsNumerous diseasesAssembly energyNeurotransmitter releaseExocytosisAttachment receptorAssemblyNeurological disordersOptical tweezersComplexesEnergetics, 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, Keun 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
2011
Cytoplasmic Permeation Pathway of Neurotransmitter Transporters
Rudnick G. Cytoplasmic Permeation Pathway of Neurotransmitter Transporters. Biochemistry 2011, 50: 7462-7475. PMID: 21774491, PMCID: PMC3164596, DOI: 10.1021/bi200926b.Peer-Reviewed Original ResearchConceptsCytoplasmic permeation pathwaysBacterial amino acid transporter LeuTNeurotransmitter transportersPermeation pathwayKingdoms of lifeMammalian serotonin transporterHigh-resolution crystal structuresFour-helix bundleRecent high-resolution crystal structureSubsequent crystal structureStructural repeatsLeuT structureProtein familyCommon structural featuresSolute transportersRelated proteinsLarge structural familyCytoplasmic oneConformational changesSubstrate siteFirst structureBiological membranesTransportersLeuTExtracellular pathways
2003
X-ray Structure of a Maquette Scaffold
Huang S, Gibney B, Stayrook S, Dutton P, Lewis M. X-ray Structure of a Maquette Scaffold. Journal Of Molecular Biology 2003, 326: 1219-1225. PMID: 12589764, DOI: 10.1016/s0022-2836(02)01441-9.Peer-Reviewed Original ResearchConceptsLeft-handed coiled-coilsCoiled-coilAnti-parallel four-helix bundleHeptad repeat patternFour-alpha-helical bundleMaquette scaffoldFour-helix bundleHeme-binding propertiesX-ray structureMAD phasingHeme binding pocketIdentical helicesResidue positionsHeptad repeatHydrophobic residuesPacking interfaceProtein scaffoldEngineering criteriaHeptadMaquettesRepeat patternHelixDesign criteriaX-rayInitial design
2000
Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1
Stebbins C, Galán J. Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1. Molecular Cell 2000, 6: 1449-1460. PMID: 11163217, DOI: 10.1016/s1097-2765(00)00141-6.Peer-Reviewed Original ResearchMeSH KeywordsAluminum CompoundsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding Sitescdc42 GTP-Binding ProteinCrystallography, X-RayDimerizationEvolution, MolecularFluoridesGTPase-Activating ProteinsGuanosine DiphosphateMacromolecular SubstancesModels, MolecularMolecular Sequence DataMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein Tyrosine Phosphatasesrac1 GTP-Binding ProteinRecombinant Fusion ProteinsSalmonella typhimuriumSequence AlignmentSignal Transduction
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