2023
Abl2 repairs microtubules and phase separates with tubulin to promote microtubule nucleation
Duan D, Lyu W, Chai P, Ma S, Wu K, Wu C, Xiong Y, Sestan N, Zhang K, Koleske A. Abl2 repairs microtubules and phase separates with tubulin to promote microtubule nucleation. Current Biology 2023, 33: 4582-4598.e10. PMID: 37858340, PMCID: PMC10877310, DOI: 10.1016/j.cub.2023.09.018.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MovementChlorocebus aethiopsCOS CellsMicrotubule-Associated ProteinsMicrotubulesTubulinConceptsCOS-7 cellsMT nucleationMT latticeFamily kinasesTubulin recruitmentLiquid-liquid phase separationTubulin C-terminal tailsCryo-EM analysisC-terminal tailAbl family kinasesWild-type cellsC-terminal halfRescue frequencyGenetic experimentsNeuronal morphogenesisMicrotubule nucleationSplice isoformsMicrotubule dynamicsNocodazole treatmentMolecular mechanismsAxon guidanceCell migrationDamage sitesABL2MT assemblyMicrotubule-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 ResearchMeSH KeywordsDyneinsHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingSaccharomyces cerevisiaeConceptsCryo-EM structureCargo transportProtein Lis1Human dyneinDynein mutantsCytoplasmic dyneinStructural insightsDynein activityIntracellular localizationCritical regulatorDynein activationLIS1Conformational changesDyneinMotor domainMutantsBindingHigh affinityAffinityYeastMicrotubulesRegulatorRegulationTransportActivation
2019
New interfaces on MiD51 for Drp1 recruitment and regulation
Ma J, Zhai Y, Chen M, Zhang K, Chen Q, Pang X, Sun F. New interfaces on MiD51 for Drp1 recruitment and regulation. PLOS ONE 2019, 14: e0211459. PMID: 30703167, PMCID: PMC6355003, DOI: 10.1371/journal.pone.0211459.Peer-Reviewed Original Research
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