2010
AS160 Associates with the Na+,K+-ATPase and Mediates the Adenosine Monophosphate-stimulated Protein Kinase-dependent Regulation of Sodium Pump Surface Expression
Alves DS, Farr GA, Seo-Mayer P, Caplan MJ. AS160 Associates with the Na+,K+-ATPase and Mediates the Adenosine Monophosphate-stimulated Protein Kinase-dependent Regulation of Sodium Pump Surface Expression. Molecular Biology Of The Cell 2010, 21: 4400-4408. PMID: 20943949, PMCID: PMC3002392, DOI: 10.1091/mbc.e10-06-0507.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsBiological TransportCell LineChlorocebus aethiopsCOS CellsDogsDose-Response Relationship, DrugEndocytosisEpithelial CellsGene ExpressionGene Knockdown TechniquesGTPase-Activating ProteinsHumansImmunoprecipitationPhosphorylationPyrazolesPyrimidinesSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsRab-GTPase-activating proteinMost epithelial cell typesCompound CProtein kinase‐dependent regulationKinase-dependent regulationActive transport proteinsMadin-Darby canine kidneyEpithelial cell typesRegulated endocytosisShort hairpin RNASurface expressionATPase endocytosisCell surface expressionProtein kinasePlasma membraneCOS cellsTransport proteinsΑ-subunitHairpin RNAAS160Cell typesIntracellular retentionVariety of mechanismsATPaseATPase activity
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
2004
Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis
Nguyen NV, Gleeson PA, Courtois-Coutry N, Caplan MJ, van Driel IR. Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis. Gastroenterology 2004, 127: 145-154. PMID: 15236181, DOI: 10.1053/j.gastro.2004.04.016.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneIntracellular traffickingTyrosine-based endocytosis motifATPase activityATPase beta subunitMembrane traffickingATPase endocytosisTrafficking eventsEndocytosis motifParietal cell ultrastructureTubulovesicular compartmentCytoplasmic tailIntracytoplasmic compartmentCl- conductanceParietal cell acid secretionBeta subunitParietal cellsDirect regulationProton pumpCell ultrastructureTraffickingATPaseCellsRegulation