2019
C‐terminal phosphorylation of latrophilin‐1/ADGRL1 affects the interaction between its fragments
Rahman M, Manser C, Benlaouer O, Suckling J, Blackburn J, Silva J, Ushkaryov Y. C‐terminal phosphorylation of latrophilin‐1/ADGRL1 affects the interaction between its fragments. Annals Of The New York Academy Of Sciences 2019, 1456: 122-143. PMID: 31553068, DOI: 10.1111/nyas.14242.Peer-Reviewed Original ResearchConceptsN-terminal fragmentG protein-coupled receptorsC-terminal fragmentLatrophilin-1Protein-coupled receptorsAdhesion G protein-coupled receptorsProtein tyrosine phosphatase σG protein-mediated signalingProtein-mediated signalingPhosphorylated C-terminal fragmentsTerminal phosphorylationIndependent proteinsPlasma membraneSeparate proteinsΑ-latrotoxinAffinity columnProteinEndocrine cellsFragmentsHigh affinityLow affinityMultiple sitesCopurifiesDephosphorylationComplexes
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 proteins
2001
A Gr receptor is required for response to the sugar trehalose in taste neurons of Drosophila
Dahanukar A, Foster K, van der Goes van Naters W, Carlson J. A Gr receptor is required for response to the sugar trehalose in taste neurons of Drosophila. Nature Neuroscience 2001, 4: 1182-1186. PMID: 11704765, DOI: 10.1038/nn765.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAnimalsAnimals, Genetically ModifiedBase SequenceBehavior, AnimalCodonDose-Response Relationship, DrugDrosophilaFood, FormulatedGene DeletionGene Expression RegulationGenetic LinkageGTP-Binding ProteinsMaleMutationNeurons, AfferentPhenotypeProtein BiosynthesisReceptors, Cell SurfaceSucroseTasteTrehaloseX ChromosomeConceptsGR geneG protein-coupled receptor genesSugar trehaloseG protein-mediated signalingDrosophila genome databaseTransgenic rescue experimentsProtein-mediated signalingSpecificity of expressionGenome databaseTaste receptorsDifferent mutantsRescue experimentsGenesLarge familyGr5aDrosophilaFunctional evidenceReceptor geneGR receptorsTaste ligandsGustatory neuronsTaste neuronsTrehaloseReceptorsFamily members
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