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 factorsPACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility
Dymek EE, Lin J, Fu G, Porter ME, Nicastro D, Smith EF. PACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility. Molecular Biology Of The Cell 2019, 30: 1805-1816. PMID: 31116684, PMCID: PMC6727744, DOI: 10.1091/mbc.e19-01-0063.Peer-Reviewed Original ResearchConceptsDoublet microtubulesAxonemal doublet microtubulesCryo-electron tomographyCiliary doublet microtubulesInner junctionCiliary assemblyCoordinated ciliary beatingFAP20Ciliary componentsMotility defectsCiliary beatingPACRGMotile ciliaFunctional studiesMutant axonemesMicrotubulesB-tubuleCiliary motilityEssential roleStructural studiesAssemblyMotilityChlamydomonasMutantsAxoneme
2018
Asymmetric distribution and spatial switching of dynein activity generates ciliary motility
Lin J, Nicastro D. Asymmetric distribution and spatial switching of dynein activity generates ciliary motility. Science 2018, 360 PMID: 29700238, PMCID: PMC6640125, DOI: 10.1126/science.aar1968.Peer-Reviewed Original ResearchConceptsDynein activitySea urchin sperm cellsCryo-electron tomographyIndividual dyneinsDynein isoformsAsymmetric distributionMotile ciliaDyneinFlagellaHypothesis positsSperm cellsSmall populationCiliary motilityFlagellar bendingCoordinated activityActive stateMotilityActivity stateOrganellesIsoformsCiliaActivityThe I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility
Fu G, Wang Q, Phan N, Urbanska P, Joachimiak E, Lin J, Wloga D, Nicastro D. The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility. Molecular Biology Of The Cell 2018, 29: mbc.e18-02-0142. PMID: 29514928, PMCID: PMC5921572, DOI: 10.1091/mbc.e18-02-0142.Peer-Reviewed Original ResearchConceptsI1 dyneinCiliary motilityAxonemal dynein motorsDynein motor domainMotor domainCiliary doublet microtubulesCK1 kinasesProper phosphorylationNormal ciliary motilityBiochemical approachesCryoelectron tomographyDynein motorsRegulatory mechanismsMotility regulatorMotile ciliaDoublet microtubulesRegulatorDyneinStable anchoringMotilityCiliary beatingComplexesHead complexMechanical feedbackImportant role
2014
Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules TEKTINS, Ca2+-BINDING PROTEINS, AND STABLE PROTOFILAMENTS* ♦
Linck R, Fu X, Lin J, Ouch C, Schefter A, Steffen W, Warren P, Nicastro D. Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules TEKTINS, Ca2+-BINDING PROTEINS, AND STABLE PROTOFILAMENTS* ♦. Journal Of Biological Chemistry 2014, 289: 17427-17444. PMID: 24794867, PMCID: PMC4067180, DOI: 10.1074/jbc.m114.568949.Peer-Reviewed Original ResearchConceptsDoublet microtubulesRibbon proteinNexin-dynein regulatory complexCiliary motilityA-tubuleIntraflagellar transportRegulatory complexAcetylated α-tubulinSignal transductionHuman homologueSpecialized functionsTektin ACalcium-binding proteinsCell organellesHuman diseasesBinding proteinΑ-tubulinΒ-tubulinSea urchin sperm flagellaSperm flagellaMicrotubule systemProteinStable protofilamentsFlagellaWide filaments
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 ResearchConceptsI1 dyneinCryoelectron tomographyGel-based proteomicsInner arm dyneinsCiliary assemblySensory organellesSubtomogram averagingDynein activityCritical regulatorDyneinPolypeptide compositionDoublet microtubulesBiochemical comparisonMotor domainCiliary motilityFlagellar beatingUnique interactionsCiliary beatingMotilityEukaryotesAssemblyChlamydomonasSubcomplexMutantsCiliopathies