2019
Serotonin and neuropeptides are both released by the HSN command neuron to initiate C. elegans egg laying
Brewer JC, Olson AC, Collins KM, Koelle MR. Serotonin and neuropeptides are both released by the HSN command neuron to initiate C. elegans egg laying. PLOS Genetics 2019, 15: e1007896. PMID: 30677018, PMCID: PMC6363226, DOI: 10.1371/journal.pgen.1007896.Peer-Reviewed Original ResearchConceptsHermaphrodite-specific neuronsEgg-laying defectsNLP-3C. elegansEgg-laying musclesEgg-laying circuitDirect postsynaptic targetsEgg-laying behaviorSerotonergic Hermaphrodite Specific NeuronsMuscle cellsSmall molecule neurotransmittersNull mutantsHSN neuronsDouble mutantSingle mutantsMutant animalsSerotonergic neuronsWild-type animalsSevere defectsMutantsElegansNeuropeptide substance PMammalian brainEggsSpecific neurons
2015
RNA ligation in neurons by RtcB inhibits axon regeneration
Kosmaczewski SG, Han SM, Han B, Meyer B, Baig HS, Athar W, Lin-Moore AT, Koelle MR, Hammarlund M. RNA ligation in neurons by RtcB inhibits axon regeneration. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 8451-8456. PMID: 26100902, PMCID: PMC4500288, DOI: 10.1073/pnas.1502948112.Peer-Reviewed Original ResearchAn Evolutionarily Conserved Switch in Response to GABA Affects Development and Behavior of the Locomotor Circuit of Caenorhabditis elegans
Han B, Bellemer A, Koelle MR. An Evolutionarily Conserved Switch in Response to GABA Affects Development and Behavior of the Locomotor Circuit of Caenorhabditis elegans. Genetics 2015, 199: 1159-1172. PMID: 25644702, PMCID: PMC4391577, DOI: 10.1534/genetics.114.173963.Peer-Reviewed Original ResearchConceptsGamma-aminobutyric acidRigorous genetic analysisBody wall musclesNeural circuit developmentCaenorhabditis elegansL1 animalsDevelopmental switchGenetic analysisGABAergic neuronsGABA responsesVertebrate brainMammalian neuronsStage animalsNeurotransmitter gamma-aminobutyric acidWall musclesChloride transportersMajor inhibitory neurotransmitterMuscle targetsTransporter 1Muscimol responsesGABA neuronsLocomotor circuitsExcitatory responsesCircuit developmentAgonist muscimol
2013
LIN-12/Notch signaling instructs postsynaptic muscle arm development by regulating UNC-40/DCC and MADD-2 in Caenorhabditis elegans
Li P, Collins KM, Koelle MR, Shen K. LIN-12/Notch signaling instructs postsynaptic muscle arm development by regulating UNC-40/DCC and MADD-2 in Caenorhabditis elegans. ELife 2013, 2: e00378. PMID: 23539368, PMCID: PMC3601818, DOI: 10.7554/elife.00378.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsCalcium SignalingCell Adhesion MoleculesFemaleGenotypeIntracellular Signaling Peptides and ProteinsMorphogenesisMuscle ContractionMusclesMutationNeurogenesisOvipositionParacrine CommunicationPhenotypeReceptors, NotchSignal TransductionSodium ChannelsSynapsesVulvaConceptsPrecise synaptic connectivityNon-target musclesForm synapsesMADD-2Types of musclePresynaptic neuronsSynaptic targetsSynaptic connectivityCardinal featuresNervous systemGuidance moleculesTarget cellsLIN-12/NotchUNC-40/DCCMuscleCell typesArm extensionCellsMuscle armsEctopic expressionDiverse cell typesDCCArmExpressionNeurons
2012
Receptors and Other Signaling Proteins Required for Serotonin Control of Locomotion in Caenorhabditis elegans
Gürel G, Gustafson MA, Pepper JS, Horvitz HR, Koelle MR. Receptors and Other Signaling Proteins Required for Serotonin Control of Locomotion in Caenorhabditis elegans. Genetics 2012, 192: 1359-1371. PMID: 23023001, PMCID: PMC3512144, DOI: 10.1534/genetics.112.142125.Peer-Reviewed Original ResearchConceptsCaenorhabditis elegansLarge-scale genetic screensSer-4Direct postsynaptic targetsGenetic screenC. elegansSignaling proteinsGenetic systemNon-overlapping setsAdditional proteinsExtrasynaptic signalsMolecular mechanismsElegansSerotonin responseGenesRelease sitesMod 1Multiple receptorsProteinSerotonin controlSerotonergic neuronsPostsynaptic targetsSerotonin functionReceptorsSerotonin receptors
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
2010
A Conserved Protein Interaction Interface on the Type 5 G Protein β Subunit Controls Proteolytic Stability and Activity of R7 Family Regulator of G Protein Signaling Proteins*
Porter MY, Xie K, Pozharski E, Koelle MR, Martemyanov KA. A Conserved Protein Interaction Interface on the Type 5 G Protein β Subunit Controls Proteolytic Stability and Activity of R7 Family Regulator of G Protein Signaling Proteins*. Journal Of Biological Chemistry 2010, 285: 41100-41112. PMID: 20959458, PMCID: PMC3003408, DOI: 10.1074/jbc.m110.163600.Peer-Reviewed Original ResearchConceptsR7 RGS proteinsG protein signaling (RGS) proteinsRGS proteinsDEP domainSignaling proteinsProtein interaction interfacesGenetic screenCaenorhabditis elegansRGS complexesObligate complexesProtein complexesFamily regulatorGβ5 proteinEquivalent mutationN-terminusConformational rearrangementsGβ5ProteinInteraction interfaceProteolysisMutationsRegulatorProteolytic stabilityComplexesDynamic opening
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 cellsProteinR7BPElegansThe Potassium Chloride Cotransporter KCC-2 Coordinates Development of Inhibitory Neurotransmission and Synapse Structure in Caenorhabditis elegans
Tanis JE, Bellemer A, Moresco JJ, Forbush B, Koelle MR. The Potassium Chloride Cotransporter KCC-2 Coordinates Development of Inhibitory Neurotransmission and Synapse Structure in Caenorhabditis elegans. Journal Of Neuroscience 2009, 29: 9943-9954. PMID: 19675228, PMCID: PMC2737711, DOI: 10.1523/jneurosci.1989-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsChloridesFurosemideHypotonic SolutionsMotor NeuronsMusclesMutationReceptors, G-Protein-CoupledSequence HomologySexual Behavior, AnimalSodium Potassium Chloride Symporter InhibitorsSymportersSynapsesSynaptic TransmissionSynaptic VesiclesUp-RegulationConceptsEgg-laying behaviorChloride channelsC. elegans behaviorGenetic screenHSN neuronsMature neural circuitsChloride gradientFunctional analysisInhibitory neurotransmissionSynapse developmentVesicle populationsAdult mammalian brainSynaptic vesicle populationPotassium-chloride cotransporterTransport chlorideSynapse maturationPotassium-chloride cotransporter KCC2CaenorhabditisAppropriate activity levelsMammalian brainSynapse structureChloride cotransporterHypotonic conditionsLoop diuretic furosemideCoordinate development
2007
C. elegans G Protein Regulator RGS-3 Controls Sensitivity to Sensory Stimuli
Ferkey DM, Hyde R, Haspel G, Dionne HM, Hess HA, Suzuki H, Schafer WR, Koelle MR, Hart AC. C. elegans G Protein Regulator RGS-3 Controls Sensitivity to Sensory Stimuli. Neuron 2007, 53: 39-52. PMID: 17196529, PMCID: PMC1855255, DOI: 10.1016/j.neuron.2006.11.015.Peer-Reviewed Original ResearchConceptsSignal transductionG protein-coupled signal transductionRGS-3G protein signaling (RGS) proteinsHeterotrimeric G proteinsSpecific RGS proteinsRGS proteinsSensory neuronsSignaling proteinsMutant animalsNegative regulatorCalcium-binding proteinsG proteinsCalcium signalingBehavioral defectsTransductionSpecific odorantsProteinDefective responseRegulatorSensory behaviorsSynaptic transmissionIntense sensory stimuliExternal stimuliSignaling
2005
Caenorhabditus elegans Arrestin Regulates Neural G Protein Signaling and Olfactory Adaptation and Recovery*
Palmitessa A, Hess HA, Bany IA, Kim YM, Koelle MR, Benovic JL. Caenorhabditus elegans Arrestin Regulates Neural G Protein Signaling and Olfactory Adaptation and Recovery*. Journal Of Biological Chemistry 2005, 280: 24649-24662. PMID: 15878875, DOI: 10.1074/jbc.m502637200.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceAnimalsAnimals, Genetically ModifiedArrestinBenzaldehydesBlotting, NorthernCaenorhabditis elegansCell LineCells, CulturedChemotaxisClathrinCOS CellsDiacetylEndocytosisExonsGreen Fluorescent ProteinsGTP-Binding ProteinsHumansImmunohistochemistryModels, GeneticMolecular Sequence DataMutationNeuronsOdorantsOlfactory PathwaysPentanolsPhenotypePhylogenyProtein BindingProtein Structure, TertiarySequence Analysis, DNASignal TransductionTime FactorsConceptsARR-1Receptor endocytosisG protein signalingG protein-coupled receptorsOlfactory adaptationVolatile odorantsProtein-coupled receptorsPotential mechanistic basisEndocytic machineryCaenorhabditis elegansNull mutantsHSN neuronsProtein signalingReceptor kinaseAdaptation defectRecovery defectArrestin functionChemosensory neuronsEnvironmental cuesBind proteinsMechanistic basisVivo linkTransgenic expressionArrestinNormal chemotaxis
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 isoformRGS-7 Completes a Receptor-Independent Heterotrimeric G Protein Cycle to Asymmetrically Regulate Mitotic Spindle Positioning in C. elegans
Hess HA, Röper JC, Grill SW, Koelle MR. RGS-7 Completes a Receptor-Independent Heterotrimeric G Protein Cycle to Asymmetrically Regulate Mitotic Spindle Positioning in C. elegans. Cell 2004, 119: 209-218. PMID: 15479638, DOI: 10.1016/j.cell.2004.09.025.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell DivisionCentrosomeEmbryo, NonmammalianGTP-Binding Protein alpha SubunitsGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHeterotrimeric GTP-Binding ProteinsMutationNuclear ProteinsProtein BindingRecombinant Fusion ProteinsRGS ProteinsRNA InterferenceSpindle ApparatusConceptsG protein functionRIC-8G proteinsProtein functionC. elegans embryosAsymmetric cell divisionG protein effectorsHeterotrimeric G proteinsMitotic spindle positioningG protein signalingG-protein cycleSeven-transmembrane receptorsGPR-1/2RGS domainElegans embryosGTPase activatorProtein effectorsProtein cycleMicrotubule forcesSpindle positioningProtein signalingCell cortexCell divisionGTP hydrolysisMitotic spindleActivation of EGL-47, a Gαo-Coupled Receptor, Inhibits Function of Hermaphrodite-Specific Motor Neurons to Regulate Caenorhabditis elegans Egg-Laying Behavior
Moresco JJ, Koelle MR. Activation of EGL-47, a Gαo-Coupled Receptor, Inhibits Function of Hermaphrodite-Specific Motor Neurons to Regulate Caenorhabditis elegans Egg-Laying Behavior. Journal Of Neuroscience 2004, 24: 8522-8530. PMID: 15456826, PMCID: PMC6729914, DOI: 10.1523/jneurosci.1915-04.2004.Peer-Reviewed Original ResearchConceptsHermaphrodite-specific neuronsEgg-laying behaviorTransmembrane domainEgg-laying defectsEgg-laying musclesDominant mutationsHSN motor neuronsFluorescent protein transgeneSixth transmembrane domainExtracellular N-terminusEgg-laying frequencyMotor neuronsN-terminusG proteinsTransgenic expressionGenesCaenorhabditisMild defectsReceptor isoformsInhibits functionMutationsMultiple receptorsEggsReceptorsNumber of neuronsMechanism 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 neuronsMutantsGenesDopamineSubunitsRegulatorGenetic Analysis of RGS Protein Function in Caenorhabditis elegans
Chase DL, Koelle MR. Genetic Analysis of RGS Protein Function in Caenorhabditis elegans. Methods In Enzymology 2004, 389: 305-320. PMID: 15313573, DOI: 10.1016/s0076-6879(04)89018-9.Peer-Reviewed Original ResearchConceptsRGS proteinsC. elegansG proteinsRGS protein functionStructure/function studiesG protein geneCaenorhabditis elegansGalpha mutantsClose homologProtein functionGalpha proteinsElegansGenetic analysisDetailed protocolTransgenic expressionProteinMost mammaliansMutantsFunction studiesOrthologsCaenorhabditisHomologMammalianGenesOrganisms
2003
Genetic and Cellular Basis for Acetylcholine Inhibition of Caenorhabditis elegans Egg-Laying Behavior
Bany IA, Dong MQ, Koelle MR. Genetic and Cellular Basis for Acetylcholine Inhibition of Caenorhabditis elegans Egg-Laying Behavior. Journal Of Neuroscience 2003, 23: 8060-8069. PMID: 12954868, PMCID: PMC6740490, DOI: 10.1523/jneurosci.23-22-08060.2003.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAcetylcholinesteraseAnimalsAnimals, Genetically ModifiedBehavior, AnimalCaenorhabditis elegansCaenorhabditis elegans ProteinsCholinesterase InhibitorsDNA, ComplementaryGTP-Binding ProteinsHomeodomain ProteinsInhibition, PsychologicalMutationNeuronsNuclear ProteinsOvipositionPhenotypeReceptors, CholinergicSignal TransductionSynapsesConceptsHermaphrodite-specific neuronsEgg-laying behaviorG proteinsG-protein signaling genesEgg-laying defectsEgg-laying musclesEgg-laying systemAnalysis of mutantsInhibition of eggSerotonergic Hermaphrodite Specific NeuronsUnc-4Caenorhabditis elegansUnc-17Signaling GenesThird cell typeActivation of eggsMorphological defectsCha-1MutantsCell typesCellular basisNeurotransmitter releaseGenesEggsPartial defect
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