0000000000077703

AUTHOR

Frans P.m. Cremers

showing 5 related works from this author

Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein.

2009

Contains fulltext : 80984.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) and Leber congenital amaurosis (LCA) are autosomal recessive disorders resulting in syndromic and non-syndromic forms of blindness. In order to gain insight into the pathogenic mechanisms underlying retinal degeneration, we searched for interacting proteins of USH2A isoform B (USH2A(isoB)) and the LCA5-encoded protein lebercilin. We identified a novel isoform of the centrosomal ninein-like protein, hereby named Nlp isoform B (Nlp(isoB)), as a common interactor. Although we identified the capacity of this protein to bind calcium with one of its three EF-hand domains, the interacton with USH2A(isoB) did …

Gene isoformRetinal degenerationCandidate geneGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeMolecular Sequence DataOptic Atrophy Hereditary LeberBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]CiliopathiesRetinaCell LineMiceCiliogenesisTwo-Hybrid System TechniquesGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansProtein IsoformsPhotoreceptor CellsAmino Acid SequenceNuclear proteinRats WistarEye ProteinsMolecular BiologyGenetics (clinical)GeneticsExtracellular Matrix ProteinsCiliumNuclear ProteinsGeneral MedicineArticlesmedicine.diseaseRatsMice Inbred C57BLMicrotubule-Associated ProteinsSequence AlignmentUsher SyndromesFunctional Neurogenomics [DCN 2]Protein BindingHuman Molecular Genetics
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Mutations in LCA5, encoding the ciliary protein lebercilin, cause Leber congenital amaurosis

2007

Contains fulltext : 53618.pdf (Publisher’s version ) (Closed access) Leber congenital amaurosis (LCA) causes blindness or severe visual impairment at or within a few months of birth. Here we show, using homozygosity mapping, that the LCA5 gene on chromosome 6q14, which encodes the previously unknown ciliary protein lebercilin, is associated with this disease. We detected homozygous nonsense and frameshift mutations in LCA5 in five families affected with LCA. In a sixth family, the LCA5 transcript was completely absent. LCA5 is expressed widely throughout development, although the phenotype in affected individuals is limited to the eye. Lebercilin localizes to the connecting cilia of photore…

MaleCandidate geneGenetics and epigenetic pathways of disease [NCMLS 6]genetic structuresMolecular Sequence DataOptic Atrophy Hereditary LeberNeuroinformatics [DCN 3]Biologymedicine.disease_causeCiliopathiesJoubert syndromeCell LineFrameshift mutationGenomic disorders and inherited multi-system disorders [IGMD 3]MiceTranslational research [ONCOL 3]Chlorocebus aethiopsPerception and Action [DCN 1]GeneticsmedicineNeurosensory disorders [UMCN 3.3]AnimalsHumansCiliaRats WistarEye ProteinsFrameshift MutationRenal disorder [IGMD 9]GeneticsMutationCiliumDisease gene identificationmedicine.diseasePhenotypeeye diseasesPedigreeRatsMice Inbred C57BLGenetic defects of metabolism [UMCN 5.1]Codon NonsenseCOS CellsFemalesense organsFunctional Neurogenomics [DCN 2]Microtubule-Associated ProteinsNature 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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Mutations in the gene encoding the basal body protein RPGRIP1L, a nephrocystin-4 interactor, cause Joubert syndrome.

2007

Peters, T.A./0000-0001-8443-5500; van Beersum, Sylvia E.C./0000-0002-4552-2908; Cremers, Frans/0000-0002-4954-5592; Roepman, Ronald/0000-0002-5178-8163 WOS: 000247619800019 PubMed: 17558407 Protein- protein interaction analyses have uncovered a ciliary and basal body protein network that, when disrupted, can result in nephronophthisis ( NPHP), Leber congenital amaurosis, Senior- Loken syndrome ( SLSN) or Joubert syndrome ( JBTS)(1-6). However, details of the molecular mechanisms underlying these disorders remain poorly understood. RPGRIP1- like protein ( RPGRIP1L) is a homolog of RPGRIP1 ( RPGR-interacting protein 1), a ciliary protein defective in Leber congenital amaurosis(7,8). We show t…

AdultMaleHealth aging / healthy living [IGMD 5]Eye DiseasesGenetics and epigenetic pathways of disease [NCMLS 6]TMEM67Molecular Sequence DataMembrane transport and intracellular motility [NCMLS 5]Biologymedicine.disease_causeJoubert syndromeCell LineGenomic disorders and inherited multi-system disorders [IGMD 3]NephronophthisisCerebellar DiseasesGeneticsmedicinePerception and Action [DCN 1]Basal bodyAnimalsHumansNeurosensory disorders [UMCN 3.3]CiliaAdaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMutationCiliumCiliary transition zoneProteinsSyndromemedicine.diseasePedigreeRatsCytoskeletal ProteinsGenetic defects of metabolism [UMCN 5.1]RPGRIP1LFemaleKidney DiseasesFunctional Neurogenomics [DCN 2]Ciliary Motility Disorders
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CNGB3 mutations account for 50% of all cases with autosomal recessive achromatopsia

2005

Contains fulltext : 47591.pdf (Publisher’s version ) (Closed access) Achromatopsia is a congenital, autosomal recessively inherited disorder characterized by a lack of color discrimination, low visual acuity (<0.2), photophobia, and nystagmus. Mutations in the genes for CNGA3, CNGB3, and GNAT2 have been associated with this disorder. Here, we analyzed the spectrum and prevalence of CNGB3 gene mutations in a cohort of 341 independent patients with achromatopsia. In 163 patients, CNGB3 mutations could be identified. A total of 105 achromats carried apparent homozygous mutations, 44 were compound (double) heterozygotes, and 14 patients had only a single mutant allele. The derived CNGB3 mutatio…

AchromatopsiaGenetics and epigenetic pathways of disease [NCMLS 6]genetic structuresGATED CATION CHANNELCNGB3 mutationsNonsense mutationMutantCyclic Nucleotide-Gated Cation ChannelsColor Vision DefectsGenes RecessiveLocus (genetics)Gene mutationBiologyTOTAL COLOURBLINDNESSIon ChannelsCLONINGDogscyclic nucleotide-gated channelGNAT2GeneticsmedicineLOCUSAnimalsHumansMissense mutationNeurosensory disorders [UMCN 3.3]ACHM3 locusDog DiseasesAlleleAllelesGenetics (clinical)Geneticstotal colorblindnessGNAT2PHOTORECEPTORSDYSTROPHYmedicine.diseaseCONE DEGENERATIONGENEeye diseasesPhenotypeEvaluation of complex medical interventions [NCEBP 2]MutationRetinal Cone Photoreceptor Cellssense organsachromatopsiarod monochromacyALPHA-SUBUNIThuman activities
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