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 interactionPP2AThe γ-Secretase Cleavage Product of Polycystin-1 Regulates TCF and CHOP-Mediated Transcriptional Activation through a p300-Dependent Mechanism
Merrick D, Chapin H, Baggs JE, Yu Z, Somlo S, Sun Z, Hogenesch JB, Caplan MJ. The γ-Secretase Cleavage Product of Polycystin-1 Regulates TCF and CHOP-Mediated Transcriptional Activation through a p300-Dependent Mechanism. Developmental Cell 2011, 22: 197-210. PMID: 22178500, PMCID: PMC3264829, DOI: 10.1016/j.devcel.2011.10.028.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid Precursor Protein SecretasesAnimalsApoptosisCell ProliferationCells, CulturedCystsEmbryo, NonmammalianHumansImmunoblottingImmunoprecipitationKidneyP300-CBP Transcription FactorsPhenotypePolycystic Kidney, Autosomal DominantTCF Transcription FactorsTranscription Factor CHOPTranscriptional ActivationTRPP Cation ChannelsWnt Signaling PathwayZebrafishConceptsCarboxy-terminal tailPolycystin-1P300-dependent mechanismTranscription factor TCFTranscriptional coactivator p300Cultured renal epithelial cellsΓ-secretase-mediated cleavageAutosomal dominant polycystic kidney diseaseRenal epithelial cellsTranscriptional activationZebrafish embryosCoactivator p300Γ-secretase activityNormal growth ratePKD1 expressionNull cellsProtein fragmentsCyst formationΓ-secretase inhibitionCHOP pathwayApoptosisEpithelial cellsCleavage productsPolycystic kidney diseaseExpressionInteractions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression
Bian S, Bai JP, Chapin H, Le Moellic C, Dong H, Caplan M, Sigworth FJ, Navaratnam DS. Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression. PLOS ONE 2011, 6: e28264. PMID: 22194818, PMCID: PMC3237428, DOI: 10.1371/journal.pone.0028264.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBeta CateninBinding SitesBiological AssayCell MembraneChickensGene Knockdown TechniquesHair Cells, AuditoryHEK293 CellsHumansImmunoprecipitationIntercellular JunctionsKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsModels, MolecularMolecular Sequence DataMutant ProteinsMutationPhosphorylationProtein BindingProtein TransportRNA, Small InterferingSequence DeletionTransfectionWnt Signaling PathwayConceptsΒ-cateninS10 regionHEK cellsSurface expressionCell biology toolsPotassium channel alpha subunitΒ-catenin interactionDownregulation of WntCytoskeleton frameworkChannel alpha subunitChicken hair cellsPhosphorylation sitesDeletion mutantsBiology toolsΒ-catenin-dependent canonical WntAlpha subunitCanonical WntMultiple binding sitesNumber of diseasesStable bindingWntPhysiological significanceBinding sitesReduced expressionHair cells
2010
Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site
Chapin HC, Rajendran V, Caplan MJ. Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site. Molecular Biology Of The Cell 2010, 21: 4338-4348. PMID: 20980620, PMCID: PMC3002387, DOI: 10.1091/mbc.e10-05-0407.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell MembraneCiliaFluorescent Antibody TechniqueHEK293 CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMutationPolycystic Kidney, Autosomal DominantProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein TransportSwineTRPP Cation ChannelsConceptsG-protein-coupled receptor proteolytic siteGPS cleavagePC2 channel activitySurface deliveryChannel activityProteolytic siteSurface localizationPlasma membrane localizationC-terminal tailHuman embryonic kidney 293 cellsEmbryonic kidney 293 cellsPC2 mutationsKidney 293 cellsMembrane localizationSecretory pathwayMembrane proteinsBinding partnerTerminal tailPolycystin-2Effect of PC2Plasma membraneCiliary membraneTRP familyLLC-PK cellsCation channelsAS160 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 activityMAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney
Carmosino M, Rizzo F, Procino G, Basco D, Valenti G, Forbush B, Schaeren-Wiemers N, Caplan MJ, Svelto M. MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney. Molecular Biology Of The Cell 2010, 21: 3985-3997. PMID: 20861303, PMCID: PMC2982131, DOI: 10.1091/mbc.e10-05-0456.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineEndocytosisEpithelial CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMembrane Transport ProteinsMiceMice, TransgenicMyelin and Lymphocyte-Associated Proteolipid ProteinsMyelin ProteinsPhosphorylationProtein BindingProteolipidsRatsRats, Inbred WKYRNA InterferenceSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 1SwineConceptsRegulation of NKCC2Apical membraneMajor salt transport pathwayC-terminal tailCell surface retentionApical sortingPorcine kidney cellsCotransporter phosphorylationTransgenic mice resultsNephron structuresRegulated absorptionImportant roleNew playersKidney cellsSurface expressionMice resultsSurface retentionTransport pathwaysNKCC2MembraneRegulationLymphocyte-associated proteinCyst formationRat kidney medullaColocalize