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
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 isoformGenetic 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
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