2022
In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts
Cai S, Wu Y, Guillén-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203769119. PMID: 35858323, PMCID: PMC9303930, DOI: 10.1073/pnas.2203769119.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCryo-focused ion beam millingMembrane contact sitesCryo-electron tomographyFull-length structureLipid transport proteinsRod-like densitiesLysosome contactBinding partnerGenetic approachesHydrophobic grooveTransport proteinsContact sitesVps13Lipid transportAlphaFold predictionsFull-length modelHeLa cellsMembrane contactSitu architectureAdjacent membranesVPS13CProteinStructural informationEndo/lysosomes
2021
Characterization of the Flagellar Collar Reveals Structural Plasticity Essential for Spirochete Motility
Chang Y, Xu H, Motaleb MA, Liu J. Characterization of the Flagellar Collar Reveals Structural Plasticity Essential for Spirochete Motility. MBio 2021, 12: e02494-21. PMID: 34809456, PMCID: PMC8609358, DOI: 10.1128/mbio.02494-21.Peer-Reviewed Original ResearchConceptsLyme disease spirochete Borrelia burgdorferiPeriplasmic flagellaSpirochete motilityCryo-electron tomographySpirochete Borrelia burgdorferiRemarkable structural plasticityComplex host environmentSerious human diseasesFlagellar assemblyCollar ComplexMultiprotein complexesFlagellar collarFlagellar motorDistinct functionsDistinct morphologiesRemarkable plasticityHuman diseasesBorrelia burgdorferiHost environmentFlagellaStructural plasticityRemarkable groupMotilityProteinHost connective tissueRole of the major determinant of polar flagellation FlhG in the endoflagella‐containing spirochete Leptospira
Fule L, Halifa R, Fontana C, Sismeiro O, Legendre R, Varet H, Coppée J, Murray GL, Adler B, Hendrixson DR, Buschiazzo A, Guo S, Liu J, Picardeau M. Role of the major determinant of polar flagellation FlhG in the endoflagella‐containing spirochete Leptospira. Molecular Microbiology 2021, 116: 1392-1406. PMID: 34657338, DOI: 10.1111/mmi.14831.Peer-Reviewed Original ResearchConceptsWild-type strainSaprophyte L. biflexaCross-species complementationComparative transcriptome analysisPathogen L. interrogansFlagellar basal bodyCryo-electron tomographySpirochete LeptospiraSpiral-shaped morphologyFlagellar genesFlhGNumerical regulationTranscriptome analysisPeriplasmic flagellaFlhFCell motilityNegative regulatorBasal bodiesBacterial speciesL. biflexaMutantsGel-like environmentL. interrogansFlagellaBacteriaSymmetrical arrangement of proteins under release-ready vesicles in presynaptic terminals
Radhakrishnan A, Li X, Grushin K, Krishnakumar SS, Liu J, Rothman JE. Symmetrical arrangement of proteins under release-ready vesicles in presynaptic terminals. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2024029118. PMID: 33468631, PMCID: PMC7865176, DOI: 10.1073/pnas.2024029118.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCryoelectron MicroscopyHippocampusImaging, Three-DimensionalMice, Inbred C57BLNerve Tissue ProteinsNeuronsPresynaptic TerminalsSynaptic VesiclesConceptsPlasma membraneSynaptic vesiclesSV fusionRelease-ready vesiclesFusion machinerySingle SNAREpinSV releaseExocytosis machineryMolecular eventsNative conditionsProtein componentsCultured hippocampal neuronsPriming reactionPresynaptic CaVesiclesFundamental processesProtein densityProtein massRelease of neurotransmittersNeurotransmitter releaseMachineryPresynaptic terminalsReleasable poolHippocampal neuronsVariable number
2020
Molecular mechanism for rotational switching of the bacterial flagellar motor
Chang Y, Zhang K, Carroll BL, Zhao X, Charon NW, Norris SJ, Motaleb MA, Li C, Liu J. Molecular mechanism for rotational switching of the bacterial flagellar motor. Nature Structural & Molecular Biology 2020, 27: 1041-1047. PMID: 32895555, PMCID: PMC8129871, DOI: 10.1038/s41594-020-0497-2.Peer-Reviewed Original ResearchConceptsBacterial flagellar motorSwitch proteinFlagellar motorResponse regulator CheYRotational switchingProton motive forceSwitch complexMolecular mechanismsPhosphorylated formMajor remodelingConformational changesMotive forceModel systemProteinBorrelia burgdorferiCheY3CheYMutantsTorque generatorFLIMInteractsCheXCW rotationMechanismRemodelingSubnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles
Li Z, Li W, Lu M, Bess J, Chao CW, Gorman J, Terry DS, Zhang B, Zhou T, Blanchard SC, Kwong PD, Lifson JD, Mothes W, Liu J. Subnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles. Nature Structural & Molecular Biology 2020, 27: 726-734. PMID: 32601441, PMCID: PMC8138683, DOI: 10.1038/s41594-020-0452-2.Peer-Reviewed Original ResearchAnalysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding
Park D, Chetrit D, Hu B, Roy CR, Liu J. Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding. MBio 2020, 11: 10.1128/mbio.03328-19. PMID: 32071271, PMCID: PMC7029142, DOI: 10.1128/mbio.03328-19.Peer-Reviewed Original ResearchConceptsType IV secretion systemSecretion systemCryoelectron tomographyInner membraneDot/Icm apparatusConformational changesDot/IcmEukaryotic host cellsBacterial inner membraneWild-type cellsHost cell membraneWhole-cell contextMultiprotein nanomachineSubtomogram analysisSophisticated nanomachinesCytoplasmic substratesProtein effectorsCell polesDNA substratesSubtomogram averagingATPase complexDNA transferHost infectionStructural basisHost cellsIn Situ Structure of the Vibrio Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator
Zhu S, Nishikino T, Takekawa N, Terashima H, Kojima S, Imada K, Homma M, Liu J. In Situ Structure of the Vibrio Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator. Journal Of Bacteriology 2020, 202: 10.1128/jb.00592-19. PMID: 31767780, PMCID: PMC6989802, DOI: 10.1128/jb.00592-19.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsCryo-electron tomographyStator unitsFlagellar rotationDetailed protein-protein interactionsUnique protein-protein interactionsGram-negative marine bacteriumPolar sheathed flagellumBasal body structureHigh-speed motilityBacterial flagellar motorLarge conformational changesSpecific interactionsFirst structural evidencePeriplasmic domainPolar flagellumFlagellar motorPeptidoglycan layerMembrane complexT ringMarine bacteriumBacterial flagellaGenetic analysisDetailed structural informationSheathed flagellum
2019
High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway
Butan C, Lara-Tejero M, Li W, Liu J, Galán JE. High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 24786-24795. PMID: 31744874, PMCID: PMC6900529, DOI: 10.1073/pnas.1916331116.Peer-Reviewed Original ResearchIn Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography
Zhu S, Schniederberend M, Zhitnitsky D, Jain R, Galán JE, Kazmierczak BI, Liu J. In Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography. Journal Of Bacteriology 2019, 201: 10.1128/jb.00117-19. PMID: 31010901, PMCID: PMC6560136, DOI: 10.1128/jb.00117-19.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyFlagellaGene Expression Regulation, BacterialPseudomonas aeruginosaSalmonella typhimuriumConceptsCryo-electron tomographyBacterial flagellaFlagellar assemblyPolar flagellumPeritrichous flagellaSerovar TyphimuriumSpecies-specific featuresBacterial pathogensOuter membrane complexSelf-assembling nanomachineFlagellar systemFlagellar structureFlagellar numberSubtomogram averagingMembrane complexLateral flagellaStructural basisDistinct flagellaMolecular machinesFlagellaSitu structureModel systemPseudomonasTyphimuriumRange of variation
2018
The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum
Zhu S, Nishikino T, Kojima S, Homma M, Liu J. The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum. Journal Of Bacteriology 2018, 200: 10.1128/jb.00387-18. PMID: 30104237, PMCID: PMC6182240, DOI: 10.1128/jb.00387-18.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyFlagellaGene DeletionGene Expression Regulation, BacterialPeriplasmVibrio alginolyticusConceptsPolar sheathed flagellumPeriplasmic flagellaExternal flagellaOuter membraneSheathed flagellumBacterial life cycleCryo-electron tomographyWild-type cellsInternal periplasmic flagellaMultiple peritrichous flagellaRemarkable nanomachinesFlagellar genesPeritrichous flagellaPeriplasmic spaceMost bacteriaNovel functionMolecular basisBacterial flagellaMajor organellesBacterial speciesFlagellaMembrane penetrationH-ringGenesLife cycleA unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel
Chetrit D, Hu B, Christie PJ, Roy CR, Liu J. A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel. Nature Microbiology 2018, 3: 678-686. PMID: 29784975, PMCID: PMC5970066, DOI: 10.1038/s41564-018-0165-z.Peer-Reviewed Original ResearchConceptsCytoplasmic complexType IV secretion channelType IV secretion systemInner membrane complexTranslocation of substratesCryo-electron tomographySecretion channelCell polesCytoplasmic ATPaseSecretion systemT4SS functionHexameric assemblyMembrane complexCytoplasmic channelsDNA complexesSubstrate transferT4SSChannel activationATPaseComplexesDistinct stagesAssemblyBiogenesisATPasesFurther analysisVisualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis
Qin Z, Hu B, Liu J. Visualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis. Methods In Molecular Biology 2018, 1729: 187-199. PMID: 29429093, DOI: 10.1007/978-1-4939-7577-8_17.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsChemotactic FactorsChemotaxisCryoelectron MicroscopyElectron Microscope TomographyHistidine KinaseSalmonella entericaSignal TransductionConceptsCryo-electron tomographyChemoreceptor arraysCheW coupling proteinLarge macromolecular assembliesChemotaxis arraysSubtomogram analysisCheA kinaseBacterial chemoreceptorsCellular contextCoupling proteinMacromolecular assembliesChemotaxis signalingMolecular levelSitu structurePrecise architectureBacterial minicellsMinicellsUnique toolKinaseSignalingProteinSubtomogramsAssemblyConcertAmplification
2017
In Situ Structural Analysis of the Spirochetal Flagellar Motor by Cryo-Electron Tomography
Zhu S, Qin Z, Wang J, Morado DR, Liu J. In Situ Structural Analysis of the Spirochetal Flagellar Motor by Cryo-Electron Tomography. Methods In Molecular Biology 2017, 1593: 229-242. PMID: 28389958, DOI: 10.1007/978-1-4939-6927-2_18.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBorrelia burgdorferiCryoelectron MicroscopyElectron Microscope TomographyFlagellaMolecular Motor ProteinsConceptsCryo-electron tomographyFlagellar motorIntact flagellar motorBacterial flagellar motorMolecular machinerySitu structural analysisExtensive structural analysisMolecular machinesLarge complexesStructural analysisUnprecedented detailBorrelia burgdorferiStructural determinationMachineryOrganismsBacteriaPowerful techniqueCellsComplexesBurgdorferiIn Situ Molecular Architecture of the Salmonella Type III Secretion Machine
Hu B, Lara-Tejero M, Kong Q, Galán JE, Liu J. In Situ Molecular Architecture of the Salmonella Type III Secretion Machine. Cell 2017, 168: 1065-1074.e10. PMID: 28283062, PMCID: PMC5393631, DOI: 10.1016/j.cell.2017.02.022.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBacterial Secretion SystemsCryoelectron MicroscopyProtein TransportSalmonella typhimuriumVirulenceConceptsType III secretion machinesSecretion machineNeedle complexType III protein secretion systemCytoplasmic sorting platformProtein secretion systemMulti-protein machinesProtein secretion machinesTarget eukaryotic cellsCryo-electron tomographyDifferent deletion mutantsSub-tomogram averagingSignificant conformational changesMolecular architectureExport apparatusEukaryotic cellsSecretion systemDeletion mutantsSorting platformConformational changesSitu structureMajor insightsMolecular modelingStructural componentsAssembly
2008
Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes
Winkler H, Zhu P, Liu J, Ye F, Roux KH, Taylor KA. Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes. Journal Of Structural Biology 2008, 165: 64-77. PMID: 19032983, PMCID: PMC2656979, DOI: 10.1016/j.jsb.2008.10.004.Peer-Reviewed Original Research
2004
A 3-D Reconstruction of Smooth Muscle α-Actinin by CryoEm Reveals Two Different Conformations at the Actin-binding Region
Liu J, Taylor DW, Taylor KA. A 3-D Reconstruction of Smooth Muscle α-Actinin by CryoEm Reveals Two Different Conformations at the Actin-binding Region. Journal Of Molecular Biology 2004, 338: 115-125. PMID: 15050827, DOI: 10.1016/j.jmb.2004.02.034.Peer-Reviewed Original Research