2013
Cornichons Control ER Export of AMPA Receptors to Regulate Synaptic Excitability
Brockie PJ, Jensen M, Mellem JE, Jensen E, Yamasaki T, Wang R, Maxfield D, Thacker C, Hoerndli F, Dunn PJ, Tomita S, Madsen DM, Maricq AV. Cornichons Control ER Export of AMPA Receptors to Regulate Synaptic Excitability. Neuron 2013, 80: 129-142. PMID: 24094107, PMCID: PMC3795439, DOI: 10.1016/j.neuron.2013.07.028.Peer-Reviewed Original ResearchConceptsGlutamatergic synaptic transmissionGlutamate-gated currentsNervous system functionIonotropic glutamate receptorsC. elegansER exportSynaptic excitabilityCargo adaptorsTransgenic wormsGenetic approachesOpposite phenotypeCornichon ProteinsGlutamate receptorsSynaptic transmissionAgonist AMPAHeterologous cellsAMPA receptorsCentral synapsesAMPAR numberSynaptic communicationReconstitution studies
2011
PDZ binding of TARPγ-8 controls synaptic transmission but not synaptic plasticity
Sumioka A, Brown TE, Kato AS, Bredt DS, Kauer JA, Tomita S. PDZ binding of TARPγ-8 controls synaptic transmission but not synaptic plasticity. Nature Neuroscience 2011, 14: 1410-1412. PMID: 22002768, PMCID: PMC3206644, DOI: 10.1038/nn.2952.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAnimalsAnimals, NewbornBiophysicsCalcium ChannelsDisks Large Homolog 4 ProteinElectric StimulationGene Expression Regulation, DevelopmentalGuanylate KinasesHippocampusIn Vitro TechniquesLong-Term PotentiationMembrane ProteinsMiceMice, TransgenicModels, BiologicalMutationNeuronal PlasticityPatch-Clamp TechniquesPDZ DomainsSynaptic TransmissionSynaptophysinSynaptosomes
1998
Cleavage of Alzheimer's Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway IDENTIFICATION OF INTRACELLULAR COMPARTMENTS IN WHICH APP CLEAVAGE OCCURS WITHOUT USING TOXIC AGENTS THAT INTERFERE WITH PROTEIN METABOLISM*
Tomita S, Kirino Y, Suzuki T. Cleavage of Alzheimer's Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway IDENTIFICATION OF INTRACELLULAR COMPARTMENTS IN WHICH APP CLEAVAGE OCCURS WITHOUT USING TOXIC AGENTS THAT INTERFERE WITH PROTEIN METABOLISM*. Journal Of Biological Chemistry 1998, 273: 6277-6284. PMID: 9497354, DOI: 10.1074/jbc.273.11.6277.Peer-Reviewed Original ResearchConceptsAlzheimer amyloid precursor proteinAmyloid precursor proteinAPP cleavageParenchymal amyloid depositsAPP carboxyl-terminal fragmentsPrecursor proteinBeta-amyloid peptideProtein metabolismNormal protein metabolismPossible intracellular siteAbeta generationAmyloid depositsAlzheimer's diseaseCarboxyl-terminal fragmentDefective O-glycosylationToxic agentsIntracellular secretory pathwayDiseasePresent studyIntracellular sitesBetaReticular compartmentAlphaCellsMetabolism