2019
FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia
Lin J, Le TV, Augspurger K, Tritschler D, Bower R, Fu G, Perrone C, O’Toole E, Mills KV, Dymek E, Smith E, Nicastro D, Porter ME. FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia. Molecular Biology Of The Cell 2019, 30: 2659-2680. PMID: 31483737, PMCID: PMC6761771, DOI: 10.1091/mbc.e19-07-0367.Peer-Reviewed Original ResearchConceptsInner dynein armsRegulatory complexCryo-electron tomographyInner arm dyneinsCiliary motilityMultiple dynein motorsPrecise spatial organizationAxonemal repeatDocking factorUnique binding siteWD repeatsDynein assemblyAssembly factorsDomain proteinsRegulatory hubDynein complexDynein isoformsDynein subunitsInsertional mutagenesisNew lociRegulatory proteinsDynein motorsDifferent dyneinsDoublet microtubulesTransport factors
2015
DRC3 connects the N-DRC to dynein g to regulate flagellar waveform
Awata J, Song K, Lin J, King SM, Sanderson MJ, Nicastro D, Witman GB. DRC3 connects the N-DRC to dynein g to regulate flagellar waveform. Molecular Biology Of The Cell 2015, 26: 2788-2800. PMID: 26063732, PMCID: PMC4571338, DOI: 10.1091/mbc.e15-01-0018.Peer-Reviewed Original Research
2014
Cryo-electron tomography reveals ciliary defects underlying human RSPH1 primary ciliary dyskinesia
Lin J, Yin W, Smith MC, Song K, Leigh MW, Zariwala MA, Knowles MR, Ostrowski LE, Nicastro D. Cryo-electron tomography reveals ciliary defects underlying human RSPH1 primary ciliary dyskinesia. Nature Communications 2014, 5: 5727. PMID: 25473808, PMCID: PMC4267722, DOI: 10.1038/ncomms6727.Peer-Reviewed Original ResearchMeSH KeywordsCiliaCryoelectron MicroscopyDNA-Binding ProteinsElectron Microscope TomographyHumansKartagener SyndromeConceptsCryo-electron tomographyNative 3D structureNormal human developmentDistant speciesHuman ciliaCilia structurePCD phenotypeCilia dysfunctionHuman diseasesNative structurePrimary ciliary dyskinesiaRadial spokesCiliaEssential roleFunctional heterogeneityHuman respiratory ciliaUnprecedented detailPrimary defectCiliary dyskinesiaUnknown primary defect
2012
Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein
Heuser T, Barber CF, Lin J, Krell J, Rebesco M, Porter ME, Nicastro D. Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: e2067-e2076. PMID: 22733763, PMCID: PMC3409752, DOI: 10.1073/pnas.1120690109.Peer-Reviewed Original ResearchMeSH KeywordsAxonemeChlamydomonasCryoelectron MicroscopyDyneinsImage Processing, Computer-AssistedImmunoblottingMicrotubulesMutationProteomicsSignal TransductionConceptsI1 dyneinCryoelectron tomographyGel-based proteomicsInner arm dyneinsCiliary assemblySensory organellesSubtomogram averagingDynein activityCritical regulatorDyneinPolypeptide compositionDoublet microtubulesBiochemical comparisonMotor domainCiliary motilityFlagellar beatingUnique interactionsCiliary beatingMotilityEukaryotesAssemblyChlamydomonasSubcomplexMutantsCiliopathies