Search results for "Centriole"

showing 10 items of 18 documents

OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar satellites and centrosomes and is mutated in one individual with oral-facial-digi…

2016

Item does not contain fulltext Oral-facial-digital (OFD) syndromes are rare heterogeneous disorders characterized by the association of abnormalities of the face, the oral cavity and the extremities, some due to mutations in proteins of the transition zone of the primary cilia or the closely associated distal end of centrioles. These two structures are essential for the formation of functional cilia, and for signaling events during development. We report here causal compound heterozygous mutations of KIAA0753/OFIP in a patient with an OFD VI syndrome. We show that the KIAA0753/OFIP protein, whose sequence is conserved in ciliated species, associates with centrosome/centriole and pericentrio…

0301 basic medicineCentriolecell-cycle progressionGene Expressionmedicine.disease_causeCiliopathieshuman-disease genemolecular characterizationbbs proteinsGenetics (clinical)Conserved SequenceCentriolesGeneticsMutationCiliumCiliary transition zoneMetabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]General MedicineOrofaciodigital Syndromes3. Good healthcentriolar satellitesmultiple sequence alignmentbasal body dockingFemaleMicrotubule-Associated ProteinsProtein BindingHeterozygoteMolecular Sequence DataBiology03 medical and health sciencesIntraflagellar transportCiliogenesis[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyGeneticsmedicineHumansAmino Acid SequenceCiliaMolecular BiologyCentrosomeintraflagellar transportBase SequenceInfant NewbornProteins030104 developmental biologyCentrosomeMutationciliary transition zoneSequence Alignment[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyciliogenesis
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Mutations in ARL2BP, Encoding ADP-Ribosylation-Factor-Like 2 Binding Protein, Cause Autosomal-Recessive Retinitis Pigmentosa

2013

Retinitis pigmentosa (RP) is a genetically heterogeneous retinal degeneration characterized by photoreceptor death, which results in visual failure. Here, we used a combination of homozygosity mapping and exome sequencing to identify mutations in ARL2BP, which encodes an effector protein of the small GTPases ARL2 and ARL3, as causative for autosomal-recessive RP (RP66). In a family affected by RP and situs inversus, a homozygous, splice-acceptor mutation, c.101−1G>C, which alters pre-mRNA splicing of ARLBP2 in blood RNA, was identified. In another family, a homozygous c.134T>G (p.Met45Arg) mutation was identified. In the mouse retina, ARL2BP localized to the basal body and cilium-associated…

AdultMaleRetinal degenerationCentrioleMolecular Sequence DataGenes RecessiveBiologymedicine.disease_causeMice03 medical and health sciences0302 clinical medicineBardet–Biedl syndromeGTP-Binding ProteinsReportRetinitis pigmentosaGeneticsmedicineAnimalsHumansBasal bodyGenetics(clinical)Photoreceptor CellsGenetics (clinical)030304 developmental biologyPrimary ciliary dyskinesiaGenetics0303 health sciencesMutationBase SequenceADP-Ribosylation FactorsCiliumHomozygoteMembrane Transport ProteinsEpithelial Cellsmedicine.diseasePedigreeCell biologyMutationFemalesense organsCarrier ProteinsRetinitis Pigmentosa030217 neurology & neurosurgeryProtein BindingTranscription FactorsThe American Journal of Human Genetics
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A novel function of Huntingtin in the cilium and retinal ciliopathy in Huntington's disease mice

2015

Huntington's disease (HD) is a neurodegenerative disorder caused by the toxic expansion of polyglutamine in the Huntingtin (HTT) protein. The pathomechanism is complex and not fully understood. Increasing evidence indicates that the loss of normal protein function also contributes to the pathogenesis, pointing out the importance of understanding the physiological roles of HTT. We provide evidence for a novel function of HTT in the cilium. HTT localizes in diverse types of cilia — including 9 + 0 non-motile sensory cilia of neurons and 9 + 2 motile multicilia of trachea and ependymal cells — which exert various functions during tissue development and homeostasis. In the photoreceptor cilium,…

AxonemeMalecongenital hereditary and neonatal diseases and abnormalitiesHuntingtinCentrioleMice TransgenicNerve Tissue ProteinsBiologyMicrotubulesPhotoreceptor cellRetinalcsh:RC321-571MiceHuntington's diseaseIntraflagellar transportmental disordersmedicineAnimalsHumansPhotoreceptor CellsHuntingtinCilialcsh:Neurosciences. Biological psychiatry. NeuropsychiatryComputingMilieux_MISCELLANEOUSHuntingtin ProteinPhotoreceptorCiliumNuclear ProteinsHuntington's diseasemedicine.diseaseCell biologyCiliopathyDisease Models Animalmedicine.anatomical_structureHEK293 CellsHuntington DiseaseNeurologyFemale[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]sense organs
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A ciliopathy complex builds distal appendages to initiate ciliogenesis

2021

ABSTRACTCells inherit two centrioles, the older of which is uniquely capable of generating a cilium. Using proteomics and super-resolved imaging, we identified a module which we term DISCO (DIStal centriole COmplex). DISCO components CEP90, MNR and OFD1 underlie human ciliopathies. This complex localized to both distal centrioles and centriolar satellites, proteinaceous granules surrounding centrioles. Cells and mice lacking CEP90 or MNR did not generate cilia, failed to assemble distal appendages, and did not transduce Hedgehog signals. Disrupting the satellite pools did not affect distal appendage assembly, indicating that it is the centriolar populations of MNR and CEP90 that are critica…

BioquímicaCentrioleGreen Fluorescent ProteinsRetinal Pigment EpitheliumBiologyCiliopathiesCell LineMice03 medical and health sciences0302 clinical medicineBacterial ProteinsGenes ReporterCiliogenesismedicineAnimalsHumansbiochemistryCiliadevelopmentHedgehogCentrioles030304 developmental biologyMice KnockoutAppendage0303 health sciencesCiliumciliaProteinsEpithelial CellscytoskeletonCell BiologyEmbryo Mammalianmedicine.diseaseCiliopathiesCell biologyMice Inbred C57BLLuminescent ProteinsCiliopathyGene Expression RegulationMicrotubule-Associated Proteins030217 neurology & neurosurgerySignal TransductionJournal of Cell Biology
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Centriolar satellites expedite mother centriole remodeling to promote ciliogenesis

2023

Centrosomes are orbited by centriolar satellites, dynamic multiprotein assemblies nucleated by Pericentriolar material 1 (PCM1). To study the requirement for centriolar satellites, we generated mice lacking PCM1, a crucial component of satellites. Pcm1−/− mice display partially penetrant perinatal lethality with survivors exhibiting hydrocephalus, oligospermia, and cerebellar hypoplasia, and variably expressive phenotypes such as hydronephrosis. As many of these phenotypes have been observed in human ciliopathies and satellites are implicated in cilia biology, we investigated whether cilia were affected. PCM1 was dispensable for ciliogenesis in many cell types, whereas Pcm1−/− multiciliated…

Cell Cycle Proteins/geneticsBiologiaGeneral Immunology and MicrobiologyCytoskeletal Proteins/metabolismGeneral NeuroscienceMothersGeneral MedicineGeneral Biochemistry Genetics and Molecular BiologyCentrioles/metabolismCentrosome/metabolismMiceCilia/metabolismAnimalsHumansFemaleeLife
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein involved in intermolecular protein interaction and microtubule association

2012

Loss-of-function mutations in the gene encoding FAM161A were recently discovered as the cause for RP28, an autosomal recessive form of retinitis pigmentosa. To initiate the characterization of the cellular role of FAM161A in the retina, we focused on its subcellular localization and conducted in vitro studies to identify FAM161A-interacting proteins and associated cellular structures. Immunohistochemistry revealed the presence of mouse FAM161A in the photoreceptor inner segments, the synaptic regions of the outer and inner plexiform layers and the ganglion cells. In mouse and human retinal sections from unfixed eyes, FAM161A localized to the ciliary region linking photoreceptor outer and in…

CentrioleImmunoelectron microscopyBiologyMicrotubulesRetinaMice03 medical and health sciences0302 clinical medicineMicrotubuleRetinitis pigmentosaGeneticsmedicineAnimalsHumansBasal bodyPhotoreceptor CellsEye ProteinsMolecular BiologyGenetics (clinical)030304 developmental biologyCentrosome0303 health sciencesRetinaCiliumGeneral Medicinemedicine.diseaseCell biologymedicine.anatomical_structureCentrosomeMutationsense organsRetinitis Pigmentosa030217 neurology & neurosurgeryHuman Molecular Genetics
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Kif3a interacts with Dynactin subunit p150 Glued to organize centriole subdistal appendages.

2013

Formation of cilia, microtubule-based structures that function in propulsion and sensation, requires Kif3a, a subunit of Kinesin II essential for intraflagellar transport (IFT). We have found that, Kif3a is also required to organize centrioles. In the absence of Kif3a, the subdistal appendages of centrioles are disorganized and lack p150(Glued) and Ninein. Consequently, microtubule anchoring, centriole cohesion and basal foot formation are abrogated by loss of Kif3a. Kif3a localizes to the mother centriole and interacts with the Dynactin subunit p150(Glued) . Depletion of p150(Glued) phenocopies the effects of loss of Kif3a, indicating that Kif3a recruitment of p150(Glued) is critical for s…

CentrioleKnockoutKinesinsBiologycentriole cohesionKif3aMedical and Health SciencesArticleGeneral Biochemistry Genetics and Molecular BiologyMiceMicrotubuleIntraflagellar transportInformation and Computing SciencesAnimalsHumansKIF3AMicrotubule anchoringMolecular BiologyCentriolesMice KnockoutGeneral Immunology and MicrobiologyGeneral NeuroscienceCiliumTumor Suppressor ProteinsNuclear ProteinsKinesinDynactin ComplexBiological SciencesCell biologyCytoskeletal ProteinscentrosomeCentrosomeHela CellsDynactinGeneric health relevanceMicrotubule-Associated Proteinsp150(Glued)HeLa Cellssubdistal appendageDevelopmental Biology
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The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium.

2010

Photoreceptors are complex ciliated sensory neurons. The basal body and periciliary ridge of photoreceptors function in association with the Golgi complex to regulate the export of proteins from the inner segment to the outer segment sensory axoneme. Here, we show that the retinitis pigmentosa protein RP2, which is a GTPase activating protein (GAP) for Arl3, localizes to the ciliary apparatus, namely the basal body and the associated centriole at the base of the photoreceptor cilium. Targeting to the ciliary base was dependent on N-terminal myristoylation. RP2 also localized to the Golgi and periciliary ridge of photoreceptors, which suggested a role for RP2 in regulating vesicle traffic an…

CentriolePhotoreceptor Connecting CiliumGolgi ApparatusBiologysymbols.namesakeMiceIntraflagellar transportGTP-Binding ProteinsGeneticsBasal bodyAnimalsHumansKIF3APhotoreceptor CellsCiliaEye ProteinsTransport VesiclesMolecular BiologyGenetics (clinical)Cells CulturedCentriolesADP-Ribosylation FactorsCiliumCiliary BodyIntracellular Signaling Peptides and ProteinsMembrane ProteinsBiological TransportGeneral MedicineGolgi apparatusCell biologysymbolssense organsCiliary baseRetinitis PigmentosaHuman molecular genetics
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Ultrastructural Pathology of Anaplastic and Grade II Ependymomas reveals Distinctive Ciliary Structures - Electron Microscopy Redux

2015

Ependymoma tumors likely derive from the ependymal cells lining the CNS ventricular system. In grade II ependymomas, tumor cells resemble typical ependymocytes, while anaplastic ependymomas are poorly differentiated. We studied three grade II and one anaplastic ependymoma, focusing on the ciliary structures. To unambiguously characterize the ultrastructure and number of cilia, we performed electron microscopy serial section analysis of individual cells. Differentiated ependymomas contained large basal bodies and up to three cilia, and lacked centrioles. Anaplastic ependymoma cells showed instead two perpendicularly oriented centrioles and lacked cilia or basal bodies. These findings could c…

EpendymomaMalePathologymedicine.medical_specialtyEpendymal CellependymomaCentrioleVentricular systemBiologyUltrastructural PathologyPathology and Forensic MedicineYoung AdultMicroscopy Electron TransmissionStructural BiologymedicineBasal bodyHumansCiliaChildelectron microscopyBrain NeoplasmsCiliumciliaAnatomyMiddle Agedmedicine.diseaseEpendymomaUltrastructureAnaplastic ependymomaFemaleNeoplasm Gradingprimary cilium
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