Search results for "Basal body"

showing 7 items of 27 documents

Germline deletion of Cetn1 causes infertility in male mice

2013

Centrins are calmodulin-like Ca2+-binding proteins that can be found in all ciliated eukaryotic cells from yeast to mammals. Expressed in male germ cells and photoreceptors, centrin 1 (CETN1) resides in the photoreceptor transition zone and connecting cilium. To identify its function in mammals, we deleted Cetn1 by homologous recombination. Cetn1−/− mice were viable and showed no sign of retina degeneration suggesting that CETN1 is nonessential for photoreceptor ciliogenesis or structural maintenance. Phototransduction components localized normally to the Cetn1−/− photoreceptor outer segments, and loss of CETN1 had no effect on light-induced translocation of transducin to the inner segment.…

Maleendocrine systemLight Signal TransductionCentrioleChromosomal Proteins Non-HistoneSpermiogenesisBiologyMice03 medical and health sciencesRetinal Rod Photoreceptor CellsCiliogenesismedicineAnimalsBasal bodyTransducinSpermatogenesisGerm-Line MutationInfertility MaleCentriolesSequence Deletion030304 developmental biologyMice KnockoutGenetics0303 health sciencesSpermatidCalcium-Binding ProteinsCell Cycle030302 biochemistry & molecular biologyCell DifferentiationCell BiologySpermatidsCell biologyMice Inbred C57BLmedicine.anatomical_structureCentrinFemalesense organsTransducinResearch ArticleVisual phototransductionJournal of Cell Science
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TALPID3 controls centrosome and cell polarity and the human ortholog KIAA0586 is mutated in Joubert syndrome (JBTS23)

2015

Joubert syndrome (JBTS) is a severe recessive neurodevelopmental ciliopathy which can affect several organ systems. Mutations in known JBTS genes account for approximately half of the cases. By homozygosity mapping and whole-exome sequencing, we identified a novel locus, JBTS23, with a homozygous splice site mutation in KIAA0586 (alias TALPID3), a known lethal ciliopathy locus in model organisms. Truncating KIAA0586 mutations were identified in two additional patients with JBTS. One mutation, c.428delG (p.Arg143Lysfs*4), is unexpectedly common in the general population and may be a major contributor to JBTS. We demonstrate KIAA0586 protein localization at the basal body in human and mouse p…

QH301-705.5chickenSciencePopulationCell Cycle ProteinsBiologymedicine.disease_causeRetinaGeneral Biochemistry Genetics and Molecular BiologyJoubert syndromeMiceTalpid3CerebellumJoubert syndromeCiliogenesismedicineAnimalsHumansBasal bodyAbnormalities MultiplehumanEye AbnormalitiesBiology (General)Human Biology and MedicineeducationmouseGeneticsMutationeducation.field_of_studyGeneral Immunology and MicrobiologyGeneral NeuroscienceCiliumQRGeneral MedicineKidney Diseases Cysticmedicine.diseaseKIAA05863. Good healthDisease Models Animalcell polarityCiliopathyDevelopmental Biology and Stem CellsciliopathycentrosomeCentrosomeMutationMedicineResearch ArticleeLife
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The mitotic spindle protein SPAG5/Astrin connects to the Usher protein network postmitotically

2011

Abstract Background Mutations in the gene for Usher syndrome 2A (USH2A) are causative for non-syndromic retinitis pigmentosa and Usher syndrome, a condition that is the most common cause of combined deaf-blindness. To gain insight into the molecular pathology underlying USH2A-associated retinal degeneration, we aimed to identify interacting proteins of USH2A isoform B (USH2AisoB) in the retina. Results We identified the centrosomal and microtubule-associated protein sperm-associated antigen (SPAG)5 in the retina. SPAG5 was also found to interact with another previously described USH2AisoB interaction partner: the centrosomal ninein-like protein NINLisoB. Using In situ hybridization, we foun…

Retinal degenerationGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeBiologyPhotoreceptor cell03 medical and health sciences0302 clinical medicineMicrotubuleEvaluation of complex medical interventions Genomic disorders and inherited multi-system disorders [NCEBP 2]Retinitis pigmentosamedicineotorhinolaryngologic diseasesBasal bodylcsh:QH573-671Ganglion cell layer030304 developmental biologyGenetics0303 health sciencesRetinalcsh:CytologyResearchPathogenesis and modulation of inflammation Infection and autoimmunity [N4i 1]Cell Biologymedicine.diseaseGenetics and epigenetic pathways of disease Plasticity and memory [NCMLS 6]eye diseasesCell biologyGenetics and epigenetic pathways of disease DCN MP - Plasticity and memory [NCMLS 6]medicine.anatomical_structure030220 oncology & carcinogenesissense organs
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TOPORS, implicated in retinal degeneration, is a cilia-centrosomal protein.

2011

et al.

Retinal degenerationUbiquitin-Protein LigasesBiologymedicine.disease_causeRetinaCell Line03 medical and health scienceschemistry.chemical_compoundMiceNuclear proteins0302 clinical medicineIntraflagellar transportGeneticsmedicineBasal bodyAnimalsHumansPhotoreceptor CellsCiliaMolecular BiologyZebrafishGenetics (clinical)Cells CulturedZebrafish030304 developmental biologyCentrosome0303 health sciencesRetinaMutationUbiquitinCiliumRetinal DegenerationNuclear ProteinsRetinalTOPORS proteinGeneral MedicineArticlesmedicine.diseasebiology.organism_classification3. Good healthCell biologyNeoplasm ProteinsProtein Transportmedicine.anatomical_structurechemistryNeoplasm proteinssense organs030217 neurology & neurosurgeryHuman molecular genetics
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MPP1 links the Usher protein network and the Crumbs protein complex in the retina.

2007

Contains fulltext : 53571.pdf (Publisher’s version ) (Closed access) The highly ordered distribution of neurons is an essential feature of a functional mammalian retina. Disruptions in the apico-basal polarity complexes at the outer limiting membrane (OLM) of the retina are associated with retinal patterning defects in vertebrates. We have analyzed the binding repertoire of MPP5/Pals1, a key member of the apico-basal Crumbs polarity complex, that has functionally conserved counterparts in zebrafish (nagie oko) and Drosophila (Stardust). We show that MPP5 interacts with its MAGUK family member MPP1/p55 at the OLM. Mechanistically, this interaction involves heterodimerization of both MAGUK mo…

Scaffold proteinanimal structuresGenetics and epigenetic pathways of disease [NCMLS 6]BioinformaticsPDZ domainMolecular Sequence DataMice TransgenicNerve Tissue ProteinsNeuroinformatics [DCN 3]Models BiologicalRetinaMiceTwo-Hybrid System TechniquesCell polarityPerception and Action [DCN 1]GeneticsNeurosensory disorders [UMCN 3.3]Basal bodyAnimalsHumansAmino Acid SequenceRats WistarEye ProteinsMolecular BiologyZebrafishGenetics (clinical)ActinRenal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsBinding SitesbiologyModels GeneticCell MembraneMembrane ProteinsGeneral MedicineBlood Proteinsbiology.organism_classificationEmbryo MammalianCell biologyProtein Structure TertiaryRatsGenetic defects of metabolism [UMCN 5.1]Eye disordersense organsCellular energy metabolism [UMCN 5.3]Nucleoside-Phosphate KinaseFunctional Neurogenomics [DCN 2]Neural developmentHuman Molecular Genetics
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Ultrastructure of Joenoides intermedia (Grassé 1952), a symbiotic parabasalid flagellate of Hodotermes mossambicus, and its comparison with other joe…

2003

Light and electron microscopy confirms the validity of the genus Joenoides. The cell is organised like other joeniids with a triangular flagellar area of about two thousand flagella/basal bodies and three privileged basal bodies located apart at the anterior corner of the flagellar area. Characteristically, the two parabasal fibres attached to the basal body #2 are very large and composed of striated subfibres that spread in the cytoplasm, where they sustain Golgi bodies. The flagellar area is surrounded by the axostylar capitulum, which is underlain by a thick layer of preaxostylar fibres, a very strongly amplified component in this species. The axostylar trunk is composed of a bundle of m…

biologyCytoplasmPeduncle (anatomy)ParabasalidUltrastructureBasal bodyAnatomyFlagellateFlagellumCytoskeletonbiology.organism_classificationMicrobiologyEuropean Journal of Protistology
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OFD1mutations in males: phenotypic spectrum and ciliary basal body docking impairment

2012

medicine.medical_specialtyRetinaCerebellumMutationCiliary basal body dockingCiliumBiologymedicine.disease_causePhenotypeCell biologyEndocrinologymedicine.anatomical_structureInternal medicineGenotypeGeneticsmedicineBasal bodyGenetics (clinical)Clinical Genetics
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