2024
Neuropeptide and serotonin co-transmission sets the activity pattern in the C. elegans egg-laying circuit
Butt A, Van Damme S, Santiago E, Olson A, Beets I, Koelle M. Neuropeptide and serotonin co-transmission sets the activity pattern in the C. elegans egg-laying circuit. Current Biology 2024, 34: 4704-4714.e5. PMID: 39395419, DOI: 10.1016/j.cub.2024.07.064.Peer-Reviewed Original ResearchHermaphrodite-specific neuronsEgg-laying circuitNlp-3Egg layingTiming of egg layingPromote egg layingCaenorhabditis elegansInactive phasePeptide signalsPersistent internal stateNeural circuit functionMolecular experimentsSerotonin receptorsSerotonin signalingSerotoninMuscle cellsNeurotransmitter serotoninMultiple signalsNeuropeptideNeuropeptide receptorsCo-transmissionEggsNeural circuitsLayingActive phaseThe Caenorhabditis elegans protein SOC-3 permits an alternative mode of signal transduction by the EGL-15 FGF receptor
Rodriguez Torres C, Wicker N, Puccini de Castro V, Stefinko M, Bennett D, Bernhardt B, Garcia Montes de Oca M, Jallow S, Flitcroft K, Palalay J, Payán Parra O, Stern Y, Koelle M, Voisine C, Woods I, Lo T, Stern M, de la Cova C. The Caenorhabditis elegans protein SOC-3 permits an alternative mode of signal transduction by the EGL-15 FGF receptor. Developmental Biology 2024, 516: 183-195. PMID: 39173814, PMCID: PMC11488645, DOI: 10.1016/j.ydbio.2024.08.014.Peer-Reviewed Original ResearchC-terminal domainEGL-15MPK-1 activationSex myoblastsSem-5CLR-1SOC-1Regulating animal developmentMode of signal transductionPTP-2Cell signaling modulatorsCell-specific differencesRAS pathway activationTissue-specific mechanismsMPK-1IRS proteinsAnimal developmentSOC-3Homeostasis defectsCaenorhabditis elegansGenetic screeningHyp7Kinase RafSignal transductionFGF signaling
2022
Horvitz, H. Robert
Koelle M. Horvitz, H. Robert. 2022 DOI: 10.1016/b978-0-12-822563-9.00005-6.ChaptersModel organism Caenorhabditis elegansForward genetic analysisOrganism Caenorhabditis elegansCaenorhabditis elegansGenetic analysisCell lineagesCell deathNormal developmentBiological researchHorvitzDisease statesAmyotrophic lateral sclerosisElegansLineagesLateral sclerosisGeneticsPhysiologyNobel PrizeCells
2021
The neural G protein Gαo tagged with GFP at an internal loop is functional in Caenorhabditis elegans
Kumar S, Olson AC, Koelle MR. The neural G protein Gαo tagged with GFP at an internal loop is functional in Caenorhabditis elegans. G3: Genes, Genomes, Genetics 2021, 11: jkab167. PMID: 34003969, PMCID: PMC8496287, DOI: 10.1093/g3journal/jkab167.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinCaenorhabditis elegansGenetic analysisHeterotrimeric G proteinsG protein GαoInternal loopC. elegansProtein complexesBiochemical purificationEpitope tagPlasma membraneAlpha subunitMolecular mechanismsFluorescent proteinGenetic studiesElegansGαoG proteinsEgg layingTransgenic expressionBiochemical studiesGαo proteinsBody morphologyProteinNeurotransmitter release
2015
Evolutionary Conservation of a GPCR-Independent Mechanism of Trimeric G Protein Activation
Coleman BD, Marivin A, Parag-Sharma K, DiGiacomo V, Kim S, Pepper JS, Casler J, Nguyen LT, Koelle MR, Garcia-Marcos M. Evolutionary Conservation of a GPCR-Independent Mechanism of Trimeric G Protein Activation. Molecular Biology And Evolution 2015, 33: 820-837. PMID: 26659249, PMCID: PMC4760084, DOI: 10.1093/molbev/msv336.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBiological EvolutionCaenorhabditis elegansCaenorhabditis elegans ProteinsEvolution, MolecularGene ExpressionGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsModels, MolecularProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein MultimerizationReceptors, G-Protein-CoupledSignal TransductionConceptsGBA motifGEF activityG protein activationTrimeric G-protein signalingGuanine nucleotide exchange factor activityProtein activationG proteinsMammalian Gα subunitsG protein-mediated signalingMotif-containing proteinsGPCR-independent mechanismReceptor-independent G-protein activationExchange factor activityG protein signalingProtein-mediated signalingMammalian cell behaviorGOA-1Evolutionary conservationDivergent proteinsCaenorhabditis elegansBioinformatics searchGα subunitsMost invertebratesProtein signalingAccessory proteinsAn 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
Postsynaptic ERG Potassium Channels Limit Muscle Excitability to Allow Distinct Egg-Laying Behavior States in Caenorhabditis elegans
Collins KM, Koelle MR. Postsynaptic ERG Potassium Channels Limit Muscle Excitability to Allow Distinct Egg-Laying Behavior States in Caenorhabditis elegans. Journal Of Neuroscience 2013, 33: 761-775. PMID: 23303953, PMCID: PMC3542984, DOI: 10.1523/jneurosci.3896-12.2013.Peer-Reviewed Original ResearchConceptsEgg-laying musclesBody bendsUNC-103Caenorhabditis elegansCalcium transientsTwo-state behaviorERG potassium channelsMutantsERG channelsPotassium channelsInactive phaseEggsDistinct behavioral statesMuscle excitabilityPostsynaptic excitabilityPostsynaptic sitesERG functionCaenorhabditisCalcium imagingElegansFurther adjustmentExcitabilityRhythmic excitationMuscleBehavioral states
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
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 cellsProteinR7BPElegansChapter 2 Insights into RGS Protein Function from Studies in Caenorhabditis elegans
Porter MY, Koelle MR. Chapter 2 Insights into RGS Protein Function from Studies in Caenorhabditis elegans. Progress In Nucleic Acid Research And Molecular Biology 2009, 86: 15-47. PMID: 20374712, DOI: 10.1016/s1877-1173(09)86002-x.Peer-Reviewed Original ResearchConceptsRGS proteinsGα proteinsMultiple RGS proteinsRGS protein functionG protein αRGS domainCaenorhabditis elegansProtein subfamiliesC. elegansGα genesProtein functionChapter 2 InsightsVivo functionNematode wormsPhysiological functionsProtein αProteinElegansSubfamiliesSuch specificityDifferent cellsRGSOrthologsCaenorhabditisMammals
2008
Regulation of Serotonin Biosynthesis by the G Proteins Gαo and Gαq Controls Serotonin Signaling in Caenorhabditis elegans
Tanis JE, Moresco JJ, Lindquist RA, Koelle MR. Regulation of Serotonin Biosynthesis by the G Proteins Gαo and Gαq Controls Serotonin Signaling in Caenorhabditis elegans. Genetics 2008, 178: 157-169. PMID: 18202365, PMCID: PMC2206068, DOI: 10.1534/genetics.107.079780.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiomarkersCaenorhabditis elegansCaenorhabditis elegans ProteinsGene Expression Regulation, EnzymologicGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11Motor NeuronsMusclesOrgan SpecificityOvipositionPromoter Regions, GeneticSerotoninSignal TransductionSynapsesTryptophan HydroxylaseConceptsEgg-laying behaviorCaenorhabditis elegansG proteinsEgg-laying systemHSN motor neuronsSerotonin biosynthesisG protein GαoLevel of transcriptionEpistasis experimentsTPH-1 expressionRate-limiting enzymeGene dosageSpecific genesGalphaoGalphaqTranscriptionBiosynthesisMotor neuronsElegansTPH-1Neurotransmitter releaseGenesMultiple signalsProteinEggs
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 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 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
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