2020
How GPCR Phosphorylation Patterns Orchestrate Arrestin-Mediated Signaling
Latorraca N, Masureel M, Hollingsworth S, Heydenreich F, Suomivuori C, Brinton C, Townshend R, Bouvier M, Kobilka B, Dror R. How GPCR Phosphorylation Patterns Orchestrate Arrestin-Mediated Signaling. Cell 2020, 183: 1813-1825.e18. PMID: 33296703, PMCID: PMC7901245, DOI: 10.1016/j.cell.2020.11.014.Peer-Reviewed Original ResearchConceptsG protein-coupled receptorsPhosphorylation patternActivation-associated conformational changesSite-directed spectroscopyPhosphorylated G protein-coupled receptorsG protein-coupled receptor phosphorylationBinding of arrestinArrestin sitesSignaling proteinsCell signalingStructural basisArrestin conformationArrestin bindingMolecular mechanismsPhosphorylationArrestinConformational changesGPCR-targeted drugsBindingBarcodingConformationProteinAtomic-level simulationsSignalPatternsMolecular mechanism of biased signaling in a prototypical G protein–coupled receptor
Suomivuori C, Latorraca N, Wingler L, Eismann S, King M, Kleinhenz A, Skiba M, Staus D, Kruse A, Lefkowitz R, Dror R. Molecular mechanism of biased signaling in a prototypical G protein–coupled receptor. Science 2020, 367: 881-887. PMID: 32079767, PMCID: PMC7259329, DOI: 10.1126/science.aaz0326.Peer-Reviewed Original ResearchConceptsMolecular dynamics simulationsAtomic-level molecular dynamics simulationsG protein-coupled receptorsExtracellular binding pocketMolecular mechanismsPrototypical G protein-coupled receptorDynamics simulationsBinding pocketLigandIntracellular conformationsAllosteric networkSignaling conformationConformationSignaling pathwayG-proteinG protein biasSignal profilesArrestinStructural mechanicsSignalReceptors
2011
Protein Phosphatase 2A Interacts with the Na+,K+-ATPase and Modulates Its Trafficking by Inhibition of Its Association with Arrestin
Kimura T, Han W, Pagel P, Nairn AC, Caplan MJ. Protein Phosphatase 2A Interacts with the Na+,K+-ATPase and Modulates Its Trafficking by Inhibition of Its Association with Arrestin. PLOS ONE 2011, 6: e29269. PMID: 22242112, PMCID: PMC3248462, DOI: 10.1371/journal.pone.0029269.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArrestinBinding, CompetitiveChlorocebus aethiopsCOS CellsG-Protein-Coupled Receptor KinasesGene DeletionHumansImmunoprecipitationKidneyMicePhosphorylationProtein BindingProtein BiosynthesisProtein Phosphatase 2Protein Structure, SecondaryProtein SubunitsProtein TransportRatsSodium-Potassium-Exchanging ATPaseConceptsC subunitATPase traffickingCatalytic subunitP-type ATPase familyG proteinsCatalytic C subunitTwo-hybrid systemIon transport proteinsEffect of arrestinNative rat kidneyATPase interactsProtein phosphataseATPase familyReceptor kinaseHomologous sequencesTransport proteinsFunctional domainsTrafficking propertiesImportant regulatorArrestinReceptor signalingIon pumpsTraffickingDirect interactionPP2A
2007
Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase
Kimura T, Allen PB, Nairn AC, Caplan MJ. Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase. Molecular Biology Of The Cell 2007, 18: 4508-4518. PMID: 17804821, PMCID: PMC2043564, DOI: 10.1091/mbc.e06-08-0711.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnimalsArrestinBinding, CompetitiveCell LineChlorocebus aethiopsChoroid PlexusCytoplasmG-Protein-Coupled Receptor KinasesKidneyMiceMicrofilament ProteinsNerve Tissue ProteinsPhosphorylationProtein BindingProtein SubunitsProtein TransportRabbitsSodium-Potassium-Exchanging ATPaseConceptsG protein-coupled receptorsLarge cytoplasmic loopExpression of spinophilinCytoplasmic loopMock-transfected cellsGRK-2Adrenergic hormonesReceptor signalingImportant modulatorSpinophilinATPase endocytosisATPase traffickingArrestin-2COS cellsArrestinHormoneAssociationATPaseGRKsCellsTraffickingEpsilonVasopressinReceptors
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
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