2009
RSBP-1 Is a Membrane-targeting Subunit Required by the Gαq-specific But Not the Gαo-specific R7 Regulator of G protein Signaling in Caenorhabditis elegans
Porter MY, Koelle MR. RSBP-1 Is a Membrane-targeting Subunit Required by the Gαq-specific But Not the Gαo-specific R7 Regulator of G protein Signaling in Caenorhabditis elegans. Molecular Biology Of The Cell 2009, 21: 232-243. PMID: 19923320, PMCID: PMC2808233, DOI: 10.1091/mbc.e09-07-0642.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell MembraneGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding Protein RegulatorsImmunoprecipitationLocomotionMembrane ProteinsMolecular Sequence DataMusclesMutationNervous SystemOvulationProtein TransportRGS ProteinsSequence AlignmentSequence Homology, Amino AcidSignal TransductionSubcellular FractionsTransgenesConceptsR7 RGS proteinsRGS proteinsCaenorhabditis elegansEGL-10EAT-16G protein signaling (RGS) proteinsG proteinsMembrane-targeting sequenceGalpha GTPase activityC. elegans neuronsPhenocopies lossR7 regulatorMembrane associationRGS activityMembrane localizationProtein familyR7 familySignaling proteinsGTPase activityPlasma membraneGenetic studiesCultured cellsProteinR7BPElegans
2007
A Specific Subset of Transient Receptor Potential Vanilloid-Type Channel Subunits in Caenorhabditis elegans Endocrine Cells Function as Mixed Heteromers to Promote Neurotransmitter Release
Jose AM, Bany IA, Chase DL, Koelle MR. A Specific Subset of Transient Receptor Potential Vanilloid-Type Channel Subunits in Caenorhabditis elegans Endocrine Cells Function as Mixed Heteromers to Promote Neurotransmitter Release. Genetics 2007, 175: 93-105. PMID: 17057248, PMCID: PMC1774992, DOI: 10.1534/genetics.106.065516.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBiological TransportCaenorhabditis elegansCaenorhabditis elegans ProteinsEndocrine GlandsFemaleIon ChannelsMolecular Sequence DataNerve Tissue ProteinsNeurosecretory SystemsOvipositionSequence Homology, Amino AcidTRPV Cation ChannelsConceptsOCR-2Neuroendocrine cellsEgg-laying defectsTRPV channel OSM-9Heteromeric channelsG protein GDominant negative mutantTransient receptor potential channelsEndocrine cell functionOSM-9Heteromeric partnerTRPV channelsSensory neuronsSingle knockoutDetectable functionOCR-1Premature eggsSensory transductionChannel subunitsDetectable roleSubunit compositionCell functionRelease of neurotransmittersNeurotransmitter releaseSubunit combinations
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 isoformMechanism of extrasynaptic dopamine signaling in Caenorhabditis elegans
Chase DL, Pepper JS, Koelle MR. Mechanism of extrasynaptic dopamine signaling in Caenorhabditis elegans. Nature Neuroscience 2004, 7: 1096-1103. PMID: 15378064, DOI: 10.1038/nn1316.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsDNA, ComplementaryDopamineGene TargetingGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsMolecular Sequence DataMotor ActivityMotor NeuronsMutationNervous SystemPhylogenyReceptors, DopamineReceptors, Dopamine D1Receptors, Dopamine D2RGS ProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidSignal TransductionConceptsCaenorhabditis elegansDOP-3DOP-1D2-like receptorsSignaling ComplexC. elegans locomotionLocomotion defectsExtrasynaptic dopamineAntagonistic effectGαoGαqElegansD2-like dopamine receptorsD1-like receptorsSame motor neuronsPathwayReceptorsDopaminergic neuronsDopamine receptorsMotor neuronsMutantsGenesDopamineSubunitsRegulator
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
2000
Multiple RGS proteins alter neural G protein signaling to allow C. elegans to rapidly change behavior when fed
Dong M, Chase D, Patikoglou G, Koelle M. Multiple RGS proteins alter neural G protein signaling to allow C. elegans to rapidly change behavior when fed. Genes & Development 2000, 14: 2003-2014. PMID: 10950865, PMCID: PMC316861, DOI: 10.1101/gad.14.16.2003.Peer-Reviewed Original ResearchConceptsRGS proteinsEGL-10Egg-laying behaviorG proteinsRGS-2RGS-1Mammalian RGS proteinsMultiple RGS proteinsHeterotrimeric G proteinsG protein GTPase activityG protein signalingProtein GTPase activityGTPase activatorCaenorhabditis elegansC. elegansRGS genesDouble mutantProtein signalingGTPase activityProteinElegansBiological purposesRegulatorAppropriate behavioral responsesEggs
1999
Antagonism between Goα and Gqα in Caenorhabditis elegans: the RGS protein EAT-16 is necessary for Goα signaling and regulates Gqα activity
Hajdu-Cronin Y, Chen W, Patikoglou G, Koelle M, Sternberg P. Antagonism between Goα and Gqα in Caenorhabditis elegans: the RGS protein EAT-16 is necessary for Goα signaling and regulates Gqα activity. Genes & Development 1999, 13: 1780-1793. PMID: 10421631, PMCID: PMC316886, DOI: 10.1101/gad.13.14.1780.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCaenorhabditis elegans ProteinsCOS CellsDNA PrimersGene Expression RegulationGenes, SuppressorGTP-Binding Protein RegulatorsGTP-Binding ProteinsHelminth ProteinsMolecular Sequence DataMutationSequence Homology, Amino AcidSignal TransductionConceptsEGL-30Cellular rolesEAT-16Double mutant analysisMajor cellular roleHeterotrimeric G proteinsG protein signalingMolecular genetic approachesCOS-7 cellsGOA-1Function mutantsCaenorhabditis elegansC. elegansDouble mutantProtein signalingGenetic approachesG proteinsSAG-1ElegansMutantsGenesGoαHyperactive phenotypeProteinMutations