2011
Two types of chloride transporters are required for GABAA receptor‐mediated inhibition in C. elegans
Bellemer A, Hirata T, Romero MF, Koelle MR. Two types of chloride transporters are required for GABAA receptor‐mediated inhibition in C. elegans. The EMBO Journal 2011, 30: 1852-1863. PMID: 21427702, PMCID: PMC3101993, DOI: 10.1038/emboj.2011.83.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, Genetically ModifiedAnion Transport ProteinsBrainCaenorhabditis elegansCaenorhabditis elegans ProteinsChloridesElectrophysiologyGene Expression RegulationHydrogen-Ion ConcentrationMicroscopyMotor ActivityMutationNeuronsOocytesPlasmidsReceptors, GABA-ASymportersTransgenesXenopusConceptsCaenorhabditis elegans mutantC. elegansSynapse developmentInhibits cellBehavioral defectsCl- gradientGABAA receptor-mediated inhibitionMutantsReceptor-mediated inhibitionTransportersChloride transportersCl- channelsIdentified mutationsNeuronal expressionCl(-) cotransporterCl(-) extruderInhibitory neurotransmissionChloride gradientChloride influxElegansCellsSevere disruptionCL flowNeural activityPrincipal mechanism
2004
Domains, Amino Acid Residues, and New Isoforms of Caenorhabditis elegans Diacylglycerol Kinase 1 (DGK-1) Important for Terminating Diacylglycerol Signaling in Vivo *
Jose AM, Koelle MR. Domains, Amino Acid Residues, and New Isoforms of Caenorhabditis elegans Diacylglycerol Kinase 1 (DGK-1) Important for Terminating Diacylglycerol Signaling in Vivo *. Journal Of Biological Chemistry 2004, 280: 2730-2736. PMID: 15563467, PMCID: PMC2048986, DOI: 10.1074/jbc.m409460200.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBinding SitesCaenorhabditis elegansCell LineCodonCodon, TerminatorDiacylglycerol KinaseDiglyceridesExonsHumansInsectaModels, GeneticMolecular Sequence DataMutationPhosphorylationPlasmidsProtein IsoformsProtein Structure, TertiaryRecombinant ProteinsSequence Homology, Amino AcidSignal TransductionConceptsCysteine-rich domainAmino acid residuesDGK-1Pleckstrin homology domainKinase domainDiacylglycerol kinaseAmino acid substitutionsAcid residuesHomology domainATP-binding site mutationsStop codonSecond cysteine-rich domainPhysiological functionsAcid substitutionsThird cysteine-rich domainHuman diacylglycerol kinaseNovel splice formsSubstituted amino acid residuesDiacylglycerol signalingPremature stop codonCaenorhabditis elegansSplice formsStop codon mutantKey residuesNew isoform
2002
An N-terminal Region of Caenorhabditis elegans RGS Proteins EGL-10 and EAT-16 Directs Inhibition of Gαo VersusGαq Signaling*
Patikoglou GA, Koelle MR. An N-terminal Region of Caenorhabditis elegans RGS Proteins EGL-10 and EAT-16 Directs Inhibition of Gαo VersusGαq Signaling*. Journal Of Biological Chemistry 2002, 277: 47004-47013. PMID: 12354761, DOI: 10.1074/jbc.m208186200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBlotting, WesternCaenorhabditis elegansCaenorhabditis elegans ProteinsCell MembraneChromosomesEpitopesGTP-Binding Protein RegulatorsHelminth ProteinsHeterotrimeric GTP-Binding ProteinsImmunoblottingModels, BiologicalMolecular Sequence DataMutationPlasmidsPromoter Regions, GeneticProtein BindingProtein Structure, TertiaryProteinsRGS ProteinsSequence Homology, Amino AcidSignal TransductionTime FactorsTransgenesConceptsN-terminal regionEGL-10EGL-30GOA-1EAT-16G protein signaling (RGS) proteinsN-terminalGPB-2RGS domainRGS proteinsC. elegansGbeta subunitsMembrane localizationSignaling proteinsN-terminal fragmentC-terminal fragmentGTPase activityTarget specificityBiochemical analysisProteinTarget selectivityFragment complexChimerasFragmentsDirect inhibition