2025
Multicilia dynamically transduce Sonic Hedgehog signaling to regulate choroid plexus functions
Mao S, Song R, Jin S, Pang S, Jovanovic A, Zimmerman A, Li P, Wu X, Wendland M, Lin K, Chen W, Choksi S, Chen G, Holtzman M, Reiter J, Wan Y, Xuan Z, Xiang Y, Xu C, Upadhyayula S, Hess H, He L. Multicilia dynamically transduce Sonic Hedgehog signaling to regulate choroid plexus functions. Cell Reports 2025, 44: 115383. PMID: 40057957, DOI: 10.1016/j.celrep.2025.115383.Peer-Reviewed Original ResearchConceptsCSF productionChoroid plexusCerebrospinal fluidSonic hedgehog signalingWater channel AQP1Increased CSF productionHedgehog signalingChoroid plexus functionMotile ciliaMulticiliaSensory ciliaShh signalingNeonatal hydrocephalusSonic hedgehogCiliary lengthRegulate CSF productionSignal intensityCiliary ultrastructureChoroidEpithelial monolayersAQP1Developmental dynamicsCiliaATP1A2PlexusPhysiologic mechanisms underlying polycystic kidney disease
Boletta A, Caplan M. Physiologic mechanisms underlying polycystic kidney disease. Physiological Reviews 2025, 105: 1553-1607. PMID: 39938884, PMCID: PMC12174308, DOI: 10.1152/physrev.00018.2024.Peer-Reviewed Original ResearchPrimary ciliaPolycystic kidney diseaseTrafficking of proteinsHuman ciliopathiesExtracellular signalsMultiple genesKidney diseaseProtein productionMolecular basisCell biologyMonogenic disordersCyst formationGenesRenal epithelial cellsProteinCiliaBiochemical informationApical surfaceEpithelial cellsFunctional expressionPhysiological propertiesWealth of informationPhysiological mechanismsCellsFibrocystin
2024
Structure, interaction and nervous connectivity of beta cell primary cilia
Müller A, Klena N, Pang S, Garcia L, Topcheva O, Aurrecoechea Duran S, Sulaymankhil D, Seliskar M, Mziaut H, Schöniger E, Friedland D, Kipke N, Kretschmar S, Münster C, Weitz J, Distler M, Kurth T, Schmidt D, Hess H, Xu C, Pigino G, Solimena M. Structure, interaction and nervous connectivity of beta cell primary cilia. Nature Communications 2024, 15: 9168. PMID: 39448638, PMCID: PMC11502866, DOI: 10.1038/s41467-024-53348-5.Peer-Reviewed Original ResearchConceptsPrimary ciliaCell's primary ciliumNon-islet cellsPancreatic beta cellsCiliary pocketSensory organellesAxonemal organizationMotility componentsExtrinsic signalsStructural basisBeta cellsCiliaCell typesExpansion microscopyParacrine signalingIslet innervationCellsIsletsBetaAxonemeOrganellesSignalThree-dimensional reconstructionInteraction
2023
CFAP45, a heterotaxy and congenital heart disease gene, affects cilia stability
Deniz E, Pasha M, Guerra M, Viviano S, Ji W, Konstantino M, Jeffries L, Lakhani S, Medne L, Skraban C, Krantz I, Khokha M. CFAP45, a heterotaxy and congenital heart disease gene, affects cilia stability. Developmental Biology 2023, 499: 75-88. PMID: 37172641, PMCID: PMC10373286, DOI: 10.1016/j.ydbio.2023.04.006.Peer-Reviewed Original ResearchConceptsLeft-right organizerCilia stabilityLeft-right patterningCongenital heart disease genesApical surfaceCell apical surfaceLive confocal imagingLeftward fluid flowHeart disease genesRecessive missense mutationLethal birth defectMotile monociliaProtein familyEarly embryogenesisMulticiliated cellsCiliary axonemeDisease genesFrog embryosGenetic underpinningsWhole-exome sequencingMissense mutationsConfocal imagingEmbryosCiliaCongenital heart diseasePleiotropic role of TRAF7 in skull-base meningiomas and congenital heart disease
Mishra-Gorur K, Barak T, Kaulen L, Henegariu O, Jin S, Aguilera S, Yalbir E, Goles G, Nishimura S, Miyagishima D, Djenoune L, Altinok S, K. D, Viviano S, Prendergast A, Zerillo C, Ozcan K, Baran B, Sencar L, Goc N, Yarman Y, Ercan-Sencicek A, Bilguvar K, Lifton R, Moliterno J, Louvi A, Yuan S, Deniz E, Brueckner M, Gunel M. Pleiotropic role of TRAF7 in skull-base meningiomas and congenital heart disease. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2214997120. PMID: 37043537, PMCID: PMC10120005, DOI: 10.1073/pnas.2214997120.Peer-Reviewed Original ResearchConceptsWild-type proteinInherited mutationsCardiac outflow tractDevelopmental heart defectsProtein functionLack ciliaPleiotropic rolesMechanistic convergenceNeural crestCiliary defectsSomatic variantsForebrain meningesCommon originDominant mannerMutationsTRAF7ZebrafishMutantsDisparate pathologiesHeterodimerizationKnockdownGeneticsProteinCiliaCongenital heart
2022
Predicting the locations of force-generating dyneins in beating cilia and flagella
Howard J, Chasteen A, Ouyang X, Geyer VF, Sartori P. Predicting the locations of force-generating dyneins in beating cilia and flagella. Frontiers In Cell And Developmental Biology 2022, 10: 995847. PMID: 36303602, PMCID: PMC9592896, DOI: 10.3389/fcell.2022.995847.Peer-Reviewed Original ResearchDynein motorsDynein motor proteinsCryogenic electron microscopyMotor proteinsCylindrical organellesDyneinSperm flagellaConformational statesFlagellaAxonemeMotile structuresCiliaThree-dimensional architectureSingle pairOrganellesATPasesIndividual motor activityProteinMolecular mechanics approachActivity changesLarge numberCellsKey questionsA serotonergic axon-cilium synapse drives nuclear signaling to alter chromatin accessibility
Sheu SH, Upadhyayula S, Dupuy V, Pang S, Deng F, Wan J, Walpita D, Pasolli HA, Houser J, Sanchez-Martinez S, Brauchi SE, Banala S, Freeman M, Xu CS, Kirchhausen T, Hess HF, Lavis L, Li Y, Chaumont-Dubel S, Clapham DE. A serotonergic axon-cilium synapse drives nuclear signaling to alter chromatin accessibility. Cell 2022, 185: 3390-3407.e18. PMID: 36055200, PMCID: PMC9789380, DOI: 10.1016/j.cell.2022.07.026.Peer-Reviewed Original ResearchConceptsCA1 pyramidal neuronsChromatin accessibilityPyramidal neuronsSerotonergic axonsEpigenetic statePrimary ciliaHippocampal CA1 pyramidal neuronsChemogenetic stimulationSerotonin receptorsNuclear actinReceptor 6Histone acetylationAxonsChemical synapsesIntercellular communicationRhoA pathwaySynapseNeuronsCiliaSynapsesStimulationPathwayNeurotransmissionReceptorsCryo-EM structure of an active central apparatus
Han L, Rao Q, Yang R, Wang Y, Chai P, Xiong Y, Zhang K. Cryo-EM structure of an active central apparatus. Nature Structural & Molecular Biology 2022, 29: 472-482. PMID: 35578022, PMCID: PMC9113940, DOI: 10.1038/s41594-022-00769-9.Peer-Reviewed Original ResearchConceptsCentral apparatusDiverse cellular activitiesKinesin-like proteinCryo-EM structureArmadillo repeat proteinsCryo-electron microscopyHigh-resolution structuresEukaryotic speciesProtein subunitsMotile ciliaBridge proteinsPair of microtubulesRegulatory roleCellular activitiesProteinDynamic conformational behaviorCiliary motilityCiliaCiliary beatingStructural frameworkConformational behaviorSubunitsMicrotubulesRegulatorSpecies
2021
Structural insights into the cause of human RSPH4A primary ciliary dyskinesia
Zhao Y, Pinskey J, Lin J, Yin W, Sears P, Daniels L, Zariwala M, Knowles M, Ostrowski L, Nicastro D. Structural insights into the cause of human RSPH4A primary ciliary dyskinesia. Molecular Biology Of The Cell 2021, 32: 1202-1209. PMID: 33852348, PMCID: PMC8351563, DOI: 10.1091/mbc.e20-12-0806.Peer-Reviewed Original ResearchConceptsStructural basisCryo-electron tomographyRadial spokesCentral pair complexUnderlying structural basisAxonemal repeatEukaryotic organellesArch domainThree-dimensional structureSubtomogram averagingOrgan positioningCell motilityStructural insightsPrimary ciliary dyskinesiaCiliaHuman ciliaHuman respiratory ciliaRS1Primary defectStructure determinationCiliary dyskinesiaHuman healthOrganellesFlagellaRepeats
2020
Regulation and function of calcium in the cilium
Sun Z. Regulation and function of calcium in the cilium. Current Opinion In Physiology 2020, 17: 278-283. PMID: 35937971, PMCID: PMC9351618, DOI: 10.1016/j.cophys.2020.08.019.Peer-Reviewed Original Research
2019
Lipid Modifications in Cilia Biology
Roy K, Marin EP. Lipid Modifications in Cilia Biology. Journal Of Clinical Medicine 2019, 8: 921. PMID: 31252577, PMCID: PMC6678300, DOI: 10.3390/jcm8070921.BooksLipid modificationCiliary proteinsCiliary protein traffickingSpecific protein poolsDifferent lipid modificationsCilia biologyProtein traffickingProtein stabilitySignaling cascadesTransporter proteinsProtein poolProteinVariety of rolesCiliaTraffickingFinal localizationCellular structureDistinctive roleBiologyRoleAbundanceModificationRegulationPathwayCascadeMechanism and Regulation of Centriole and Cilium Biogenesis
Breslow DK, Holland AJ. Mechanism and Regulation of Centriole and Cilium Biogenesis. Annual Review Of Biochemistry 2019, 88: 1-34. PMID: 30601682, PMCID: PMC6588485, DOI: 10.1146/annurev-biochem-013118-111153.ChaptersConceptsInterphase microtubule cytoskeletonMicrotubule-based organellesBiogenesis of centriolesMost animal cellsCore of centrosomesFormation of ciliaNine-fold symmetryCilia biologyCilia biogenesisCellular signalingMicrotubule cytoskeletonAnimal cellsMitotic spindleBasal bodiesHuman diseasesCentriolesBiogenesisRegulatory controlCentral roleCiliaExciting avenuesCentrosomesCytoskeletonOrganellesSignaling
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 stateOrganellesIsoformsCiliaActivityA CRISPR-based screen for Hedgehog signaling provides insights into ciliary function and ciliopathies
Breslow DK, Hoogendoorn S, Kopp AR, Morgens DW, Vu BK, Kennedy MC, Han K, Li A, Hess GT, Bassik MC, Chen JK, Nachury MV. A CRISPR-based screen for Hedgehog signaling provides insights into ciliary function and ciliopathies. Nature Genetics 2018, 50: 460-471. PMID: 29459677, PMCID: PMC5862771, DOI: 10.1038/s41588-018-0054-7.Peer-Reviewed Original ResearchConceptsFunctional genomic screensGenome-wide CRISPRCiliary functionHedgehog-responsive cellsCiliary signalingΕ-tubulinProtein complexesGenomic screenEmbryonic developmentGene disruptionPrimary ciliaΔ-tubulinNovel componentCiliopathiesCRISPRCiliary structureUnbiased toolHedgehogUnifying causeScreenGenesSignalingCiliaSystematic analysisPathway
2017
Palmitoylation of the ciliary GTPase ARL13b is necessary for its stability and its role in cilia formation
Roy K, Jerman S, Jozsef L, McNamara T, Onyekaba G, Sun Z, Marin EP. Palmitoylation of the ciliary GTPase ARL13b is necessary for its stability and its role in cilia formation. Journal Of Biological Chemistry 2017, 292: 17703-17717. PMID: 28848045, PMCID: PMC5663873, DOI: 10.1074/jbc.m117.792937.Peer-Reviewed Original ResearchConceptsPost-translational attachmentMost mammalian cellsCiliary GTPase Arl13bCilia localizationProtein palmitoylationCiliary proteinsCilia proteinsProtein localizationCilia formationMammalian cellsCilia functionPalmitoylationPrimary ciliaPlasma membraneCilia resorptionArl13bFunctional importanceMyristoylationCiliaCritical roleProteinMouse kidneyLocalizationDepalmitoylationCellsCiliary Mechanisms of Cyst Formation in Polycystic Kidney Disease
Ma M, Gallagher AR, Somlo S. Ciliary Mechanisms of Cyst Formation in Polycystic Kidney Disease. Cold Spring Harbor Perspectives In Biology 2017, 9: a028209. PMID: 28320755, PMCID: PMC5666631, DOI: 10.1101/cshperspect.a028209.Peer-Reviewed Original ResearchConceptsPolycystin-2Autosomal dominant polycystic kidney diseaseCalcium-mediated signalsRole of ciliaDisruption of ciliaPolycystic kidney diseaseCellular processesCausal genesTransmembrane proteinTissue homeostasisCilia functionPrimary ciliaPolycystinsGenetic studiesHomeostatic maintenanceSignal integrationUnknown mechanismApical surfaceNephron structuresCiliaKidney tubule cellsIntact ciliaPrivileged compartmentActive remodelingTubule structure
2016
Digenic mutations of human OCRL paralogs in Dent’s disease type 2 associated with Chiari I malformation
Duran D, Jin SC, DeSpenza T, Nelson-Williams C, Cogal AG, Abrash EW, Harris PC, Lieske JC, Shimshak SJ, Mane S, Bilguvar K, DiLuna ML, Günel M, Lifton RP, Kahle KT. Digenic mutations of human OCRL paralogs in Dent’s disease type 2 associated with Chiari I malformation. Human Genome Variation 2016, 3: 16042. PMID: 28018608, PMCID: PMC5143364, DOI: 10.1038/hgv.2016.42.Peer-Reviewed Original ResearchDigenic mutationsPH domainPrimary ciliaDamaging missense mutationsGenetic supportINPP5BSilico analysisMutation impactOCRL1Amino acidsMissense mutationsParalogsBp deletionMutationsCiliogenesisExon 3Novel associationsAbove-average IQVariable presencePhosphatidylinositolPolyPhen2MetaSVMSequencingDeletionCiliaThe IN/OUT assay: a new tool to study ciliogenesis
Kukic I, Rivera-Molina F, Toomre D. The IN/OUT assay: a new tool to study ciliogenesis. Cilia 2016, 5: 23. PMID: 27493724, PMCID: PMC4972980, DOI: 10.1186/s13630-016-0044-2.Peer-Reviewed Original ResearchCiliary pocketCiliary transmembrane proteinsPlasma membrane invaginationsDeep plasma membrane invaginationsPrimary cilia assemblyCilia assemblyMembrane invaginationsTransmembrane proteinPrimary ciliaCellular antennaCilia lengthMolecular characterizationMost ciliaFunctional studiesCiliogenesisCiliaNew toolRPE cellsCellsAssaysAntibody accessEHD1New assayPocketConventional assays
2015
The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135
Stoops EH, Hull M, Olesen C, Mistry K, Harder JL, Rivera-Molina F, Toomre D, Caplan MJ. The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135. Journal Of Cell Biology 2015, 211: 287-294. PMID: 26504168, PMCID: PMC4621837, DOI: 10.1083/jcb.201502045.Peer-Reviewed Original ResearchConceptsPrimary ciliaSurface proteinsTrans-Golgi networkPolarized epithelial cellsApical surface proteinsSNAP-tag systemBasolateral plasma membraneCell surface proteinsEpithelial cellsApical proteinsPericiliary regionGolgi networkPolarized traffickingCarrier vesiclesProtein deliveryPlasma membraneApical membraneProteinGp135Basolateral membraneCiliaMembraneHot spotsCellsTraffickingPhosphoinositide 3-Kinase-C2α Regulates Polycystin-2 Ciliary Entry and Protects against Kidney Cyst Formation
Franco I, Margaria JP, De Santis MC, Ranghino A, Monteyne D, Chiaravalli M, Pema M, Campa CC, Ratto E, Gulluni F, Perez-Morga D, Somlo S, Merlo GR, Boletta A, Hirsch E. Phosphoinositide 3-Kinase-C2α Regulates Polycystin-2 Ciliary Entry and Protects against Kidney Cyst Formation. Journal Of The American Society Of Nephrology 2015, 27: 1135-1144. PMID: 26271513, PMCID: PMC4814170, DOI: 10.1681/asn.2014100967.Peer-Reviewed Original ResearchConceptsPI3K-C2αCiliary componentsPolycystin-2Primary ciliaRecycling endosome compartmentKidney cyst formationDuct 3 cellsCiliary entryCilium baseElongation defectsCargo proteinsCilium morphogenesisSubcellular locationPhosphoinositide 3Endosome compartmentTubule developmentProliferation signalsCiliary transportCyst formationCystic kidney diseaseIschemia/reperfusion-induced renal damageGenetic modelsCiliaCyst developmentKey mediator
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