2003
Derangements of Hippocampal Calcium/Calmodulin-Dependent Protein Kinase II in a Mouse Model for Angelman Mental Retardation Syndrome
Weeber EJ, Jiang YH, Elgersma Y, Varga AW, Carrasquillo Y, Brown SE, Christian JM, Mirnikjoo B, Silva A, Beaudet AL, Sweatt JD. Derangements of Hippocampal Calcium/Calmodulin-Dependent Protein Kinase II in a Mouse Model for Angelman Mental Retardation Syndrome. Journal Of Neuroscience 2003, 23: 2634-2644. PMID: 12684449, PMCID: PMC6742065, DOI: 10.1523/jneurosci.23-07-02634.2003.Peer-Reviewed Original ResearchMeSH KeywordsAngelman SyndromeAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCells, CulturedHippocampusImmunohistochemistryIntellectual DisabilityLigasesLong-Term PotentiationMiceMutationPhosphoprotein PhosphatasesPhosphorylationProtein KinasesSynapsesThreonineUbiquitin-Protein LigasesConceptsCalmodulin-dependent protein kinase IIProtein kinase IIKinase IIAngelman syndromeCalcium/calmodulin-dependent protein kinase IIMutant animalsMolecular basisMental retardation syndromeMolecular causesCaMKII activityLong-term potentiationCaMKIIPostsynaptic densityRetardation syndromeMouse modelMisregulationMutantsHippocampal long-term potentiationSevere mental retardationMental retardationContext-dependent learningCorresponding changesRequirement of e6ap and the features of human papillomavirus e6 necessary to support degradation of p53
Cooper B, Schneider S, Bohl J, Jiang Y, Beaudet A, Pol S. Requirement of e6ap and the features of human papillomavirus e6 necessary to support degradation of p53. Virology 2003, 306: 87-99. PMID: 12620801, DOI: 10.1016/s0042-6822(02)00012-0.Peer-Reviewed Original Research
2002
Genetic Ablation of the Steroid Receptor Coactivator-Ubiquitin Ligase, E6-AP, Results in Tissue-Selective Steroid Hormone Resistance and Defects in Reproduction
Smith CL, DeVera DG, Lamb DJ, Nawaz Z, Jiang YH, Beaudet AL, O’Malley B. Genetic Ablation of the Steroid Receptor Coactivator-Ubiquitin Ligase, E6-AP, Results in Tissue-Selective Steroid Hormone Resistance and Defects in Reproduction. Molecular And Cellular Biology 2002, 22: 525-535. PMID: 11756548, PMCID: PMC139730, DOI: 10.1128/mcb.22.2.525-535.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDrug ResistanceFemaleFertilityGene ExpressionGrowthHistone AcetyltransferasesLigasesMaleMammary Glands, AnimalMiceMice, Inbred C57BLMice, KnockoutNuclear Receptor Coactivator 1Nuclear Receptor Coactivator 3PregnancyProstateReceptors, SteroidReproductionSteroidsTrans-ActivatorsTranscription FactorsUbiquitin-Protein LigasesConceptsSteroid hormone actionWild-type controlsHormone actionProstate gland growthFemale knockout miceSteroid hormone resistanceE6-APSex steroid actionSteroid receptor coactivatorVirgin mammary glandMammary gland developmentReceptor-dependent gene expressionFemale miceUterine growthHormone resistanceSteroid actionKnockout miceNull miceGland growthType 1Genetic ablationMammary glandReceptor coactivatorMiceGland development
1999
Mutation of the E6-AP Ubiquitin Ligase Reduces Nuclear Inclusion Frequency While Accelerating Polyglutamine-Induced Pathology in SCA1 Mice
Cummings C, Reinstein E, Sun Y, Antalffy B, Jiang Y, Ciechanover A, Orr H, Beaudet A, Zoghbi H. Mutation of the E6-AP Ubiquitin Ligase Reduces Nuclear Inclusion Frequency While Accelerating Polyglutamine-Induced Pathology in SCA1 Mice. Neuron 1999, 24: 879-892. PMID: 10624951, DOI: 10.1016/s0896-6273(00)81035-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxin-1AtaxinsCell NucleusCells, CulturedCysteine EndopeptidasesFluorescent Antibody TechniqueHeLa CellsHumansImmunoblottingImmunohistochemistryInclusion BodiesLigasesMiceMice, KnockoutMicroscopy, ConfocalMultienzyme ComplexesMutationNerve Tissue ProteinsNuclear ProteinsPeptidesPhenotypePlasmidsProteasome Endopeptidase ComplexPurkinje CellsSpinocerebellar DegenerationsUbiquitin-Protein LigasesUbiquitinsConceptsMutant ataxin-1Ataxin-1Spinocerebellar ataxia type 1Ataxin-1 aggregationUbiquitin-protein ligaseUbiquitin-positive nuclear inclusionsUbiquitin-proteasome pathwayNuclear inclusionsPolyglutamine proteinsProteasomal degradationProteasome distributionMutant formsSCA1 pathogenesisAtaxia type 1Patient neuronsPurkinje cell pathologySCA1 miceCell pathologyInclusion frequencyCellsLigasePurkinje cellsProteinPaternal Deletion from Snrpn to Ube3a in the Mouse Causes Hypotonia, Growth Retardation and Partial Lethality and Provides Evidence for a Gene Contributing to Prader-Willi Syndrome
Tsai T, Jiang Y, Bressler J, Armstrong D, Beaudet A. Paternal Deletion from Snrpn to Ube3a in the Mouse Causes Hypotonia, Growth Retardation and Partial Lethality and Provides Evidence for a Gene Contributing to Prader-Willi Syndrome. Human Molecular Genetics 1999, 8: 1357-1364. PMID: 10400982, DOI: 10.1093/hmg/8.8.1357.Peer-Reviewed Original ResearchMeSH KeywordsAbnormalities, MultipleAnimalsAutoantigensBrainChromosome DeletionFemaleGene ExpressionGenomic ImprintingHumansLigasesMaleMiceMice, Inbred StrainsMuscle HypotoniaMutagenesis, Site-DirectedOpen Reading FramesPedigreePhenotypePrader-Willi SyndromeRibonucleoproteins, Small NuclearRNASnRNP Core ProteinsUbiquitin-Protein LigasesConceptsOpen reading framePartial lethalityExon 2Pathogenesis of PWSUpstream open reading framesObvious phenotypic abnormalitiesMouse chromosome 7CGenomic imprintsImprinted expressionPrader-Willi syndromeHuman translocationImprinted genesGene ContributingStructural genePaternal deficiencyChromosome 7CPaternal chromosomesGenotype/phenotype correlationHuman chromosomesMethylation patternsImprinting mutationsReading frameMultiple genesLoss of expressionSNRPNGenetics of Angelman Syndrome
Jiang Y, Lev-Lehman E, Bressler J, Tsai T, Beaudet A. Genetics of Angelman Syndrome. American Journal Of Human Genetics 1999, 65: 1-6. PMID: 10364509, PMCID: PMC1378067, DOI: 10.1086/302473.Peer-Reviewed Original Research
1998
Mutation of the Angelman Ubiquitin Ligase in Mice Causes Increased Cytoplasmic p53 and Deficits of Contextual Learning and Long-Term Potentiation
Jiang Y, Armstrong D, Albrecht U, Atkins C, Noebels J, Eichele G, Sweatt J, Beaudet A. Mutation of the Angelman Ubiquitin Ligase in Mice Causes Increased Cytoplasmic p53 and Deficits of Contextual Learning and Long-Term Potentiation. Neuron 1998, 21: 799-811. PMID: 9808466, DOI: 10.1016/s0896-6273(00)80596-6.Peer-Reviewed Original ResearchConceptsLong-term potentiationMaternal deficiencyAngelman syndromeNormal baseline synaptic transmissionBaseline synaptic transmissionE6-AP ubiquitinMotor dysfunctionSynaptic transmissionPhenotype of miceMice causesPotential biochemical basisPostmitotic neuronsLearning deficitsMiceDegradation of p53E6 proteinPotentiationP53Cytoplasmic p53UBE3ACytoplasmic abundanceDeficitsDeficiencyPhenotypeBiochemical basisImprinting in Angelman and Prader-Willi syndromes
Jiang Y, Tsai T, Bressler J, Beaudet A. Imprinting in Angelman and Prader-Willi syndromes. Current Opinion In Genetics & Development 1998, 8: 334-342. PMID: 9691003, DOI: 10.1016/s0959-437x(98)80091-9.Peer-Reviewed Original ResearchConceptsE6-AP ubiquitin-protein ligaseUbiquitin-protein ligaseAnalysis of methylationTissue-specific imprintingAngelman syndromeSNRPN promoterPrader-Willi syndromeAS genesMaternal chromosomesGene expressionGenomic sequencingPoint mutationsGenesBisulfite methodMethylationCandidate regionsImprintingHippocampal neuronsDrosophilaNecdinSNRPNLigaseChromosomesPromoterPurkinje cells
1997
The E6–AP Ubiquitin–Protein Ligase (UBE3A) Gene Is Localized within a Narrowed Angelman Syndrome Critical Region
Sutcliffe J, Jiang Y, Galjaard R, Matsuura T, Fang P, Kubota T, Christian S, Bressler J, Cattanach B, Ledbetter D, Beaudet A. The E6–AP Ubiquitin–Protein Ligase (UBE3A) Gene Is Localized within a Narrowed Angelman Syndrome Critical Region. Genome Research 1997, 7: 368-377. PMID: 9110176, PMCID: PMC139148, DOI: 10.1101/gr.7.4.368.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAngelman SyndromeAnimalsBlotting, NorthernBlotting, SouthernChromosome AberrationsChromosome MappingChromosomes, Artificial, YeastChromosomes, Human, Pair 15Cloning, MolecularCosmidsElectrophoresis, Gel, Pulsed-FieldFemaleGene DeletionGene DosageGene Expression Regulation, DevelopmentalGenetic MarkersGenomic ImprintingHumansIn Situ HybridizationLigasesMaleMiceMice, Mutant StrainsMolecular Sequence DataPaternityPrader-Willi SyndromeSequence Homology, Amino AcidSequence Homology, Nucleic AcidTissue DistributionTranscription, GeneticTranslocation, GeneticUbiquitin-Protein LigasesConceptsLigase geneUbiquitin protein ligase geneAngelman syndromeEntire transcriptional unitCandidate regionsMaternal-specific expressionE6-AP ubiquitinTranscriptional unitsPaternal deficiencyRT-PCR analysisMouse homologPrader-Willi syndromePaternal uniparental disomyPhysical mapDe novo truncating mutationsNovo truncating mutationsRecent identificationUBE3A locusMouse tissuesGenesUbe3a expressionLociUniparental disomyProtein levelsAS regionDe novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome
Matsuura T, Sutcliffe J, Fang P, Galjaard R, Jiang Y, Benton C, Rommens J, Beaudet A. De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome. Nature Genetics 1997, 15: 74-77. PMID: 8988172, DOI: 10.1038/ng0197-74.Peer-Reviewed Original ResearchConceptsGene productsAngelman syndromeNovo truncating mutationsUbiquitin protein ligase geneUbiquitin-dependent proteolytic pathwayE6-AP ubiquitin-protein ligaseHuman genetic disordersUbiquitin-protein ligaseUBE3A geneTruncating mutationsEvidence of expressionUnlikely candidate geneGenetic disordersLigase geneParental allelesAS genesHuman chromosomesPaternal uniparental disomyCandidate genesDe novo truncating mutationsProteolytic pathwayNovo nonsense mutationGenesIntragenic mutationsMolecular defects