Search results for "Usher Syndromes"

showing 10 items of 25 documents

Mutation profile of the MYO7A gene in Spanish patients with Usher syndrome type I.

2006

Usher syndrome type I is the most severe form of Usher syndrome. It is an autosomal recessive disorder characterized by profound congenital sensorineural deafness, retinitis pigmentosa, and vestibular abnormalities. Mutations in the myosin VIIA gene (MYO7A) are responsible for Usher syndrome type 1B (USH1B). This gene is thought to bear greatest responsibility for USH1 and, depending on the study, has been reported to account for between 24% and 59% of USH1 cases. In this report a mutation screening of the MYO7A gene was carried out in a series of 48 unrelated USH1 families using single strand conformation polymorphism analysis (SSCP) and direct sequencing of those fragments showed an abnor…

MYO7AUsher syndromeDNA Mutational AnalysisBiologyMyosinsFrameshift mutationRetinitis pigmentosaotorhinolaryngologic diseasesGeneticsmedicineMissense mutationHumansGenetic Predisposition to DiseaseGeneGenetics (clinical)Polymorphism Single-Stranded ConformationalGeneticsPolymorphism GeneticModels GeneticDyneinsSingle-strand conformation polymorphismmedicine.diseaseeye diseasesStop codonGene Expression RegulationSpainMyosin VIIaMutationUsher SyndromesHuman mutation
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Homozygous disruption of PDZD7 by reciprocal translocation in a consanguineous family: a new member of the Usher syndrome protein interactome causing…

2008

A homozygous reciprocal translocation, 46,XY,t(10;11),t(10;11), was detected in a boy with non-syndromic congenital sensorineural hearing impairment. Both parents and their four other children were heterozygous translocation carriers, 46,XX,t(10;11) and 46,XY,t(10;11), respectively. Fluorescence in situ hybridization of region-specific clones to patient chromosomes was used to localize the breakpoints within bacterial artificial chromosome (BAC) RP11-108L7 on chromosome 10q24.3 and within BAC CTD-2527F12 on chromosome 11q23.3. Junction fragments were cloned by vector ligation and sequenced. The chromosome 10 breakpoint was identified within the PDZ domain containing 7 (PDZD7) gene, disrupti…

MaleCandidate geneHeterozygoteUsher syndromePDZ domainMolecular Sequence DataChromosomal translocationBiologyTranslocation GeneticConsanguinityotorhinolaryngologic diseasesGeneticsmedicineHumansAmino Acid SequenceHearing LossMolecular BiologyGenetics (clinical)GeneticsGene RearrangementBacterial artificial chromosomemedicine.diagnostic_testBase SequenceChromosomes Human Pair 10Chromosomes Human Pair 11BreakpointHomozygoteChromosomeGeneral Medicinemedicine.diseaseMolecular biologyPedigreeChild PreschoolEar InnerFemaleUsher SyndromesFluorescence in situ hybridizationHuman molecular genetics
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Functional analysis of splicing mutations in MYO7A and USH2A genes.

2010

Usher syndrome is defined by the association of sensorineural hearing loss, retinitis pigmentosa and variable vestibular dysfunction. Many disease-causative mutations have been identified in MYO7A and USH2A genes, which play a major role in Usher syndrome type I and type II, respectively. The pathogenic nature of mutations that lead to premature stop codons is not questioned; nevertheless, additional studies are needed to verify the pathogenicity of some changes such as those putatively involved in the splice process. Five putative splice-site variants were detected in our cohort of patients: c.2283-1G>T and c.5856G>A in MYO7A and c.1841-2A>G, c.2167+5G>A and c.5298+1G>C in the USH2A gene. …

MaleGenotypeUsher syndromeRNA SplicingBiologyMyosinsmedicine.disease_causeExonChlorocebus aethiopsGene OrderGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansspliceGeneGenetics (clinical)GeneticsMutationExtracellular Matrix Proteinsmedicine.diseaseStop codonMyosin VIIaRNA splicingCOS CellsMutationFemaleRNA Splice SitesUsher SyndromesMinigeneClinical genetics
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The giant spectrin βV couples the molecular motors to phototransduction and Usher syndrome type I proteins along their trafficking route.

2013

International audience; Mutations in the myosin VIIa gene cause Usher syndrome type IB (USH1B), characterized by deaf-blindness. A delay of opsin trafficking has been observed in the retinal photoreceptor cells of myosin VIIa-deficient mice. We identified spectrin bV, the mammalian b-heavy spectrin, as a myosin VIIa-and rhodopsin-interacting partner in photoreceptor cells. Spectrin bV displays a polarized distribution from the Golgi apparatus to the base of the outer segment, which, unlike that of other b spectrins, matches the trafficking route of opsin and other phototransduction proteins. Formation of spectrin bV-rhodopsin complex could be detected in the differentiating photoreceptors a…

OpsinRhodopsinLight Signal Transductiongenetic structures[SDV]Life Sciences [q-bio]Cell Cycle Proteinsmacromolecular substancesBiologyMyosinsOpsin transportRetinaMotor protein03 medical and health sciencesMice0302 clinical medicineMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansSpectrinMolecular BiologyGenetics (clinical)030304 developmental biologyAdaptor Proteins Signal Transducing0303 health sciencesEPB41SpectrinGeneral Medicineeye diseasesCell biologyCytoskeletal ProteinsRhodopsinMyosin VIIabiology.proteinMicrotubule Proteinssense organsUsher Syndromes030217 neurology & neurosurgeryVisual phototransductionHeLa CellsPhotoreceptor Cells VertebrateHuman molecular genetics
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AAV-Mediated Clarin-1 Expression in the Mouse Retina: Implications for USH3A Gene Therapy

2015

Usher syndrome type III (USH3A) is an autosomal recessive disorder caused by mutations in clarin-1 (CLRN1) gene, leading to progressive retinal degeneration and sensorineural deafness. Efforts to develop therapies for preventing photoreceptor cell loss are hampered by the lack of a retinal phenotype in the existing USH3 mouse models and by conflicting reports regarding the endogenous retinal localization of clarin-1, a transmembrane protein of unknown function. In this study, we used an AAV-based approach to express CLRN1 in the mouse retina in order to determine the pattern of its subcellular localization in different cell types. We found that all major classes of retinal cells express AAV…

Photoreceptors0301 basic medicineRetinal degenerationSensory ReceptorsPhysiologyUsher syndromeCell Membraneslcsh:MedicineSocial SciencesNervous SystemPhotoreceptor cellMicechemistry.chemical_compound0302 clinical medicineAnimal CellsMedicine and Health SciencesPsychologylcsh:ScienceNeuronsRegulation of gene expressionGeneticsMultidisciplinaryRetinal DegenerationAnimal ModelsDependovirusCell biologyElectrophysiologymedicine.anatomical_structureSensory PerceptionCellular TypesAnatomyCellular Structures and OrganellesUsher SyndromesResearch ArticleSignal TransductionCell typeImaging TechniquesOcular AnatomyNeurophysiologyOuter plexiform layerMouse ModelsBiologyResearch and Analysis MethodsRetina03 medical and health sciencesModel OrganismsOcular SystemFluorescence ImagingmedicineAnimalsHumansRetinalcsh:RMembrane ProteinsBiology and Life SciencesAfferent NeuronsRetinalGenetic TherapyCell Biologymedicine.diseaseDisease Models Animal030104 developmental biologyGene Expression RegulationchemistrySynapsesEyeslcsh:QHead030217 neurology & neurosurgeryNeurosciencePLOS ONE
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SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
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SANS (USH1G) expression in developing and mature mammalian retina

2008

AbstractThe human Usher syndrome (USH) is the most common form of combined deaf-blindness. Usher type I (USH1), the most severe form, is characterized by profound congenital deafness, constant vestibular dysfunction and prepubertal-onset of retinitis pigmentosa. Five corresponding genes of the six USH1 genes have been cloned so far. The USH1G gene encodes the SANS (scaffold protein containing ankyrin repeats and SAM domain) protein which consists of protein motifs known to mediate protein–protein interactions. Recent studies indicated SANS function as a scaffold protein in the protein interactome related to USH.Here, we generated specific antibodies for SANS protein expression analyses. Our…

Retinal degenerationScaffold proteinBlotting WesternNerve Tissue ProteinsBiologyRibbon synapseRats Inbred WKYPhotoreceptor cellRetinaMiceXenopus laevisAntibody SpecificityCiliogenesisConnecting ciliumRetinitis pigmentosamedicineAnimalsCiliaEye ProteinsCentrosomeRetinaCiliogenesisPhotoreceptor cellsCiliumImmune SeraCiliary BodyFibroblastsmedicine.diseaseSynapseSensory SystemsCell biologyRatsMice Inbred C57BLOphthalmologymedicine.anatomical_structureSynapsesRetinal developmentsense organsUsher SyndromesUsher syndromePhotoreceptor Cells VertebrateSynaptosomesVision Research
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Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2.

2005

Contains fulltext : 48386.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) is the most frequent cause of combined deaf-blindness in man. USH is clinically and genetically heterogeneous with at least 11 chromosomal loci assigned to the three USH types (USH1A-G, USH2A-C, USH3A). Although the different USH types exhibit almost the same phenotype in human, the identified USH genes encode for proteins which belong to very different protein classes and families. We and others recently reported that the scaffold protein harmonin (USH1C-gene product) integrates all identified USH1 molecules in a USH1-protein network. Here, we investigated the relationship between the USH2 molecules a…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeStereocilia (inner ear)Cell Cycle ProteinsBiologyInteractomeReceptors G-Protein-CoupledMiceotorhinolaryngologic diseasesGeneticsmedicineAnimalsNeurosensory disorders [UMCN 3.3]Photoreceptor CellsRats WistarMolecular BiologyGeneGenetics (clinical)Renal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsStereociliumBinding SitesHair Cells Auditory InnerSodium-Bicarbonate SymportersUsher Syndrome Type 1General Medicinemedicine.diseasePhenotypeRatsMice Inbred C57BLCytoskeletal ProteinsCarrier ProteinsUsher Syndromes
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A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.

2008

Contains fulltext : 69178.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic anal…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]XenopusCell Cycle ProteinsNerve Tissue ProteinsBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]TransfectionModels BiologicalReceptors G-Protein-CoupledMiceChlorocebus aethiopsProtein Interaction MappingGeneticsPerception and Action [DCN 1]otorhinolaryngologic diseasesAnimalsHumansNeurosensory disorders [UMCN 3.3]Cell Cycle ProteinMicroscopy ImmunoelectronMolecular BiologyIntegral membrane proteinGenetics (clinical)Adaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMice KnockoutExtracellular Matrix ProteinsCiliumSignal transducing adaptor proteinMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyMice Inbred C57BLCytoskeletal ProteinsEctodomainGenetic defects of metabolism [UMCN 5.1]COS CellsNIH 3T3 CellsCervical collarUsher SyndromesFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateSubcellular FractionsImmunity infection and tissue repair [NCMLS 1]
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Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-mediated endocytosis.

2014

Item does not contain fulltext The human Usher syndrome (USH) is a complex ciliopathy with at least 12 chromosomal loci assigned to three clinical subtypes, USH1-3. The heterogeneous USH proteins are organized into protein networks. Here, we identified Magi2 (membrane-associated guanylate kinase inverted-2) as a new component of the USH protein interactome, binding to the multifunctional scaffold protein SANS (USH1G). We showed that the SANS-Magi2 complex assembly is regulated by the phosphorylation of an internal PDZ-binding motif in the sterile alpha motif domain of SANS by the protein kinase CK2. We affirmed Magi2's role in receptor-mediated, clathrin-dependent endocytosis and showed tha…

Scaffold proteinGuanylate kinaseMolecular Sequence DataPrimary Cell CultureNerve Tissue ProteinsBiologyEndocytosisPhotoreceptor cellExocytosisMiceCiliogenesisGeneticsmedicineAnimalsHumansProtein Interaction Domains and MotifsAmino Acid SequencePhosphorylationRNA Small InterferingSensory disorders Radboud Institute for Molecular Life Sciences [Radboudumc 12]Molecular BiologyGenetics (clinical)Adaptor Proteins Signal TransducingBinding SitesGeneral MedicineClathrinEndocytosisCell biologyMice Inbred C57BLRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]medicine.anatomical_structureHEK293 CellsGene Expression RegulationCiliary pocketCarrier ProteinsSterile alpha motifGuanylate KinasesSequence AlignmentUsher SyndromesPhotoreceptor Cells VertebrateProtein BindingSignal TransductionHuman molecular genetics
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