2017
GARLH Family Proteins Stabilize GABAA Receptors at Synapses
Yamasaki T, Hoyos-Ramirez E, Martenson JS, Morimoto-Tomita M, Tomita S. GARLH Family Proteins Stabilize GABAA Receptors at Synapses. Neuron 2017, 93: 1138-1152.e6. PMID: 28279354, PMCID: PMC5347473, DOI: 10.1016/j.neuron.2017.02.023.Peer-Reviewed Original ResearchConceptsInhibitory transmissionSynaptic transmissionSynaptic localizationInhibitory synaptic transmissionFast inhibitory transmissionFast synaptic transmissionIonotropic neurotransmitter receptorsLigand-gated ion channelsAuxiliary subunitsGABAA receptorsIonotropic GABANeurotransmitter receptorsNeuroligin-2GABAReceptorsAnion channelIon channelsBrainHippocampusFindingsSynapses
2014
Synaptic localization of neurotransmitter receptors: comparing mechanisms for AMPA and GABAA receptors
Martenson JS, Tomita S. Synaptic localization of neurotransmitter receptors: comparing mechanisms for AMPA and GABAA receptors. Current Opinion In Pharmacology 2014, 20: 102-108. PMID: 25529200, PMCID: PMC4318715, DOI: 10.1016/j.coph.2014.11.011.Peer-Reviewed Original ResearchConceptsSynaptic localizationBasal transmissionGABAA receptorsSynaptic transmissionAMPA receptorsNeurotransmitter receptorsSynaptic plasticityFast synaptic transmissionMultiple receptor subunitsIonotropic neurotransmitter receptorsSynaptic insertionReceptor numberReceptor subunitsReceptorsPrecise mechanismReceptor propertiesAuxiliary subunitsTARP auxiliary subunitsRecent findingsDistinct mechanismsAMPAPostsynapsesPlasticitySynapsesPharmacology
2011
Distinct functions of kainate receptors in the brain are determined by the auxiliary subunit Neto1
Straub C, Hunt DL, Yamasaki M, Kim KS, Watanabe M, Castillo PE, Tomita S. Distinct functions of kainate receptors in the brain are determined by the auxiliary subunit Neto1. Nature Neuroscience 2011, 14: 866-873. PMID: 21623363, PMCID: PMC3125417, DOI: 10.1038/nn.2837.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornBiophysical PhenomenaBiophysicsCA1 Region, HippocampalCell Line, TransformedCerebellumDisks Large Homolog 4 ProteinDizocilpine MaleateDose-Response Relationship, DrugDrug InteractionsElectric StimulationExcitatory Amino Acid AgonistsExcitatory Amino Acid AntagonistsExcitatory Postsynaptic PotentialsGene Expression RegulationGreen Fluorescent ProteinsGuanylate KinasesHumansImmunoprecipitationIn Vitro TechniquesIntracellular Signaling Peptides and ProteinsKainic AcidLDL-Receptor Related ProteinsLipoproteins, LDLMembrane PotentialsMembrane ProteinsMiceMice, KnockoutNeuronsPatch-Clamp TechniquesPresynaptic TerminalsProtein BindingProtein SubunitsReceptors, Kainic AcidReceptors, N-Methyl-D-AspartateSynaptophysinTransfectionTritium
2010
Hippocampal AMPA Receptor Gating Controlled by Both TARP and Cornichon Proteins
Kato AS, Gill MB, Ho MT, Yu H, Tu Y, Siuda ER, Wang H, Qian YW, Nisenbaum ES, Tomita S, Bredt DS. Hippocampal AMPA Receptor Gating Controlled by Both TARP and Cornichon Proteins. Neuron 2010, 68: 1082-1096. PMID: 21172611, PMCID: PMC3034222, DOI: 10.1016/j.neuron.2010.11.026.Peer-Reviewed Original ResearchConceptsTransmembrane AMPA receptor regulatory proteinsAMPA receptor complexesHippocampal neuronsAMPA receptorsCornichon ProteinsReceptor complexAMPA receptor traffickingReceptor regulatory proteinsGlutamate applicationKnockout miceTARP γReceptor pharmacologyCNIH-2Electrophysiological propertiesPostsynaptic densityAMPA receptor gatingSubunit combinationsProtein levelsResensitizationReceptor traffickingNeuronsPharmacologyReceptorsReceptor gatingRecombinant systems
2000
Regulation of X11L-dependent Amyloid Precursor Protein Metabolism by XB51, a Novel X11L-binding Protein*
Lee D, Tomita S, Kirino Y, Suzuki T. Regulation of X11L-dependent Amyloid Precursor Protein Metabolism by XB51, a Novel X11L-binding Protein*. Journal Of Biological Chemistry 2000, 275: 23134-23138. PMID: 10833507, DOI: 10.1074/jbc.c000302200.Peer-Reviewed Original ResearchOverexpression of Human Amyloid Precursor Protein in Drosophila
Yagi Y, Tomita S, Nakamura M, Suzuki T. Overexpression of Human Amyloid Precursor Protein in Drosophila. Archives Of Biochemistry And Biophysics 2000, 4: 43-49. PMID: 11152627, DOI: 10.1006/mcbr.2000.0248.Peer-Reviewed Original ResearchConceptsHuman APPHuman amyloid precursor proteinAPP expression levelsExpression of APPPrecursor proteinAmyloid precursor proteinBeta-amyloid peptideSynaptic terminalsHuman neuronsAlzheimer's diseaseNeural cellsApp functionsExpression levelsDiseasePhysiological functionsProtein transport systemWing blister phenotypePhenotypeWing phenotypeImaginal discsCuticle secretionNeuronsWing tissueProteinSecretionPDZ Domain-dependent Suppression of NF-κB/p65-induced Aβ42 Production by a Neuron-specific X11-like Protein*
Tomita S, Fujita T, Kirino Y, Suzuki T. PDZ Domain-dependent Suppression of NF-κB/p65-induced Aβ42 Production by a Neuron-specific X11-like Protein*. Journal Of Biological Chemistry 2000, 275: 13056-13060. PMID: 10777610, DOI: 10.1074/jbc.c000019200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlzheimer DiseaseAmyloid beta-PeptidesAnimalsBrainCell LineCOS CellsDNA, ComplementaryGene Expression RegulationGene LibraryHumansLuciferasesNerve Tissue ProteinsNeuronsNF-kappa BNF-kappa B p50 SubunitPeptide FragmentsPrecipitin TestsProtein BindingProtein IsoformsProtein Structure, TertiaryTranscription Factor RelATranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsNF-kappaB/p65X11-like proteinsAlzheimer's diseaseNF-kappaB/p50Progression of ADAmyloid precursor proteinSpecific therapyAbeta productionAβ42 productionAbeta42 productionNF-kappaBP65Neuronal cellsAmino acids 161Precursor proteinX11LAbeta42DiseaseRel homology domainSecretionX11L.P50LIN-10Transcription factorsTherapy
1999
Interaction of a Neuron-specific Protein Containing PDZ Domains with Alzheimer's Amyloid Precursor Protein*
Tomita S, Ozaki T, Taru H, Oguchi S, Takeda S, Yagi Y, Sakiyama S, Kirino Y, Suzuki T. Interaction of a Neuron-specific Protein Containing PDZ Domains with Alzheimer's Amyloid Precursor Protein*. Journal Of Biological Chemistry 1999, 274: 2243-2254. PMID: 9890987, DOI: 10.1074/jbc.274.4.2243.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlzheimer DiseaseAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsChromosome MappingChromosomes, Human, Pair 9Cloning, MolecularDNA, ComplementaryHumansMolecular Sequence DataNerve Tissue ProteinsNeuronsProtein BindingProtein Processing, Post-TranslationalSequence Homology, Amino Acid
1998
A Basic Amino Acid in the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein (APP) Is Essential for Cleavage of APP at the α-Site*
Tomita S, Kirino Y, Suzuki T. A Basic Amino Acid in the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein (APP) Is Essential for Cleavage of APP at the α-Site*. Journal Of Biological Chemistry 1998, 273: 19304-19310. PMID: 9668120, DOI: 10.1074/jbc.273.30.19304.Peer-Reviewed Original ResearchConceptsAlzheimer's β-Amyloid Precursor ProteinΒ-amyloid precursor proteinAlzheimer's diseaseSecretion of Abeta40Beta-amyloid precursor proteinFamilial AD mutationsPrecursor proteinAPP cytoplasmic domainBeta-amyloid peptideAPP metabolismAD mutationsSporadic typeAbeta productionAberrant metabolismCTFbetaIntracellular accumulationBasic amino acidsAmino acid mutationsAmino acidsDiseaseSingle amino acid mutationNon-basic amino acidsMetabolismAcid mutationsCytoplasmic domainCleavage 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 compartmentAlphaCellsMetabolismcDNA isolation of Alzheimer's amyloid precursor protein from cholinergic nerve terminals of the electric organ of the electric ray
IIJIMA K, LEE D, OKUTSU J, TOMITA S, HIRASHIMA N, KIRINO Y, SUZUKI T. cDNA isolation of Alzheimer's amyloid precursor protein from cholinergic nerve terminals of the electric organ of the electric ray. Biochemical Journal 1998, 330: 29-33. PMID: 9461486, PMCID: PMC1219103, DOI: 10.1042/bj3300029.Peer-Reviewed Original ResearchConceptsAlzheimer amyloid precursor proteinAmyloid precursor proteinNerve terminalsCholinergic nerve terminalsPrecursor proteinBeta-amyloid domainAPP695 isoformCholinergic neuronsElectric ray electric organCell bodiesElectric organNeuronsRay electric organPresent studyElectric lobePhosphorylation sitesCytoplasmic domainOrgansPhosphorylated formPhosphorylationProtein