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 CellsGene DeletionG-Protein-Coupled Receptor KinasesHumansImmunoprecipitationKidneyMicePhosphorylationProtein 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
1999
Nongastric H+,K+-ATPase: cell biologic and functional properties.
Grishin AV, Reinhard J, Dunbar LA, Courtois-Coutry N, Wang T, Giebisch G, Caplan MJ. Nongastric H+,K+-ATPase: cell biologic and functional properties. Seminars In Nephrology 1999, 19: 421-30. PMID: 10511382.Peer-Reviewed Original ResearchConceptsATPase isoformsP-type ATPasesEndocytic regulationEndocytosis signalATPase familyCell machineryCytoplasmic tailK resorptionATPasesIon pumpsATPase isoform expressionApical surfaceIsoformsCell biologicIsoform expressionPhysiological studiesTubule epithelial cellsATPaseEpithelial cellsTransgenic miceCation transportK transportFunctional propertiesRenal K transportEndocytosis