2023
Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport
Ton W, Wang Y, Chai P, Beauchamp-Perez C, Flint N, Lammers L, Xiong H, Zhang K, Markus S. Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport. Nature Structural & Molecular Biology 2023, 30: 1365-1379. PMID: 37322240, PMCID: PMC10590275, DOI: 10.1038/s41594-023-01010-x.Peer-Reviewed Original ResearchConceptsCryo-EM structureCargo transportProtein Lis1Human dyneinDynein mutantsCytoplasmic dyneinStructural insightsDynein activityIntracellular localizationCritical regulatorDynein activationLIS1Conformational changesDyneinMotor domainMutantsBindingHigh affinityAffinityYeastMicrotubulesRegulatorRegulationTransportActivationHigh-Resolution Structural Analysis of Dyneins by Cryo-electron Microscopy
Chai P, Rao Q, Wang Y, Zhang K. High-Resolution Structural Analysis of Dyneins by Cryo-electron Microscopy. Methods In Molecular Biology 2023, 2623: 257-279. PMID: 36602691, PMCID: PMC10371436, DOI: 10.1007/978-1-0716-2958-1_16.ChaptersConceptsCryo-electron microscopyHigh-resolution structural informationLarge molecular machineHigh-resolution structuresCryo-EM approachResolution structural analysisProtein complexesStructural biologistsCellular cargoMolecular machinesDyneinDepth mechanistic understandingMolecular motorsMechanistic understandingCiliary motilityFlexible conformationIntricate architectureStructural informationMacromolecular structureForce generatorStructural analysisBiologistsSimilar structureCargoMicroscopy
2021
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism
Rao Q, Han L, Wang Y, Chai P, Kuo YW, Yang R, Hu F, Yang Y, Howard J, Zhang K. Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism. Nature Structural & Molecular Biology 2021, 28: 799-810. PMID: 34556869, PMCID: PMC8500839, DOI: 10.1038/s41594-021-00656-9.Peer-Reviewed Original ResearchConceptsOuter arm dyneinMicrotubule doubletsDistinct microtubule-binding domainsHigh-resolution structuresAction of dyneinsMicrotubule-binding domainNative tracksATP hydrolysisDynein motorsHydrolyze ATPConformational changesNucleotide cycleMotor coordination mechanismATP turnoverDyneinHead interactionsMechanical forces
2017
Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated
Zhang K, Foster HE, Rondelet A, Lacey SE, Bahi-Buisson N, Bird AW, Carter AP. Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated. Cell 2017, 169: 1303-1314.e18. PMID: 28602352, PMCID: PMC5473941, DOI: 10.1016/j.cell.2017.05.025.Peer-Reviewed Original ResearchConceptsStructure-based mutagenesisCryoelectron microscopy structureCargo adaptor proteinsMicroscopy structureAdaptor proteinCytoplasmic dyneinMicrotubule affinityCryo-EMDynein 1DynactinOpen formDynein tailInhibited stateProcessive movementMotor domainMicrotubulesMotor dimerizationTransport machinesHigh affinityMutagenesisDyneinTailAffinityProteinDimerization
2015
The structure of the dynactin complex and its interaction with dynein
Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP. The structure of the dynactin complex and its interaction with dynein. Science 2015, 347: 1441-1446. PMID: 25814576, PMCID: PMC4413427, DOI: 10.1126/science.aaa4080.Peer-Reviewed Original ResearchConceptsDynactin complexBicaudal D2Microtubule motors cytoplasmic dynein-1Distinct protein complexesCytoplasmic dynein-1Cryo-electron microscopyProtein Arp1Protein complexesAngstrom structureDynein 1DynactinEssential cofactorΒ-actinDyneinShoulder domainDependent interactionFilamentsComplexesArp1CofactorActinCopiesInteractionPeptidesDomain