2011
Interactions 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
2000
The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*
Asano S, Kawada K, Kimura T, Grishin A, Caplan M, Takeguchi N. The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*. Journal Of Biological Chemistry 2000, 275: 8324-8330. PMID: 10722662, DOI: 10.1074/jbc.275.12.8324.Peer-Reviewed Original ResearchConceptsAlpha/beta assemblyN-glycosylation sitesATPase activityBeta assemblyPutative N-glycosylation sitesCarbohydrate chainsAlpha/beta complexSingle carbohydrate chainCatalytic subunitSurface deliveryFunctional enzymeAsparagine residuesAlpha subunitΒ-subunitBeta complexDelivery mechanismFunctional expressionComplete lossATPaseAssemblyExpressionSubunitsA Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase
Dunbar L, Aronson P, Caplan M. A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase. Journal Of Cell Biology 2000, 148: 769-778. PMID: 10684257, PMCID: PMC2169368, DOI: 10.1083/jcb.148.4.769.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCationsCell LineCell MembraneCell PolarityGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationMembrane ProteinsMolecular Sequence DataOuabainParietal Cells, GastricProtein Sorting SignalsRecombinant Fusion ProteinsSequence AlignmentSequence DeletionSodium-Potassium-Exchanging ATPaseSolubilityTransfectionConceptsK-ATPase alpha subunitAlpha subunitTransmembrane domainPolytopic membrane transport proteinK-ATPaseApical distributionGlycosphingolipid-rich membrane domainsDetergent-insoluble complexesMembrane transport proteinsApical membrane proteinsApical plasma membraneK-ATPase alphaFourth transmembrane domainLocalization signalChimeric pumpsFourth transmembraneTransmembrane segmentsK-ATPase sequencesMembrane compartmentsMembrane domainsMembrane proteinsSequence domainsPlasma membraneGastric parietal cellsTransport proteins
1998
Effects of okadaic acid, calyculin A, and PDBu on state of phosphorylation of rat renal Na+-K+-ATPase
Li D, Cheng S, Fisone G, Caplan M, Ohtomo Y, Aperia A. Effects of okadaic acid, calyculin A, and PDBu on state of phosphorylation of rat renal Na+-K+-ATPase. American Journal Of Physiology 1998, 275: f863-f869. PMID: 9843902, DOI: 10.1152/ajprenal.1998.275.6.f863.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDopamine and cAMP-Regulated Phosphoprotein 32Dose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsIn Vitro TechniquesKidneyMaleMarine ToxinsNerve Tissue ProteinsOkadaic AcidOxazolesPhorbol 12,13-DibutyratePhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Kinase CRatsRats, Sprague-DawleySodium-Potassium-Exchanging ATPaseConceptsState of phosphorylationOkadaic acidPP-2ACalyculin AProtein kinasePP-1PP-1 activityATPase alpha subunitProtein kinase C activatorProtein phosphatasePresence of PDBuAlpha subunitATPase phosphorylationPhosphorylationC activatorProtein 1Anti-alpha antibodyATPaseATPase activityKinaseSuch regulationPDBu inhibitionPDBuPhosphataseFK-506
1993
Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly
Gottardi CJ, Caplan MJ. Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly. Journal Of Biological Chemistry 1993, 268: 14342-14347. PMID: 8390991, DOI: 10.1016/s0021-9258(19)85246-8.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitK-ATPase beta subunitAlpha subunitBeta subunitCell surface expressionTerminal halfK-ATPaseCell surface deliveryEfficient cell surface expressionK-ATPase alphaNH2-terminal halfCOS-1 cellsIon-transporting ATPasesProtein domainsK-ATPase enzymeSubunit assemblySurface deliveryIntracellular vesiclesSubunit chimerasIndividual subunitsActive enzymeMolecular requirementsSubunitsCell surfaceBeta protein
1992
Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture.
Pietrini G, Matteoli M, Banker G, Caplan MJ. Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8414-8418. PMID: 1326755, PMCID: PMC49930, DOI: 10.1073/pnas.89.18.8414.Peer-Reviewed Original ResearchConceptsHippocampal neuronsAlpha 1Epithelial cellsMature cultured hippocampal neuronsCultured hippocampal neuronsK-ATPase alpha subunitPolarized epithelial cell lineAlpha 3 proteinAlpha 3 isoformDistribution of isoformsEpithelial cell lineRenal epithelial cellsInfluenza glycoproteinsVesicular stomatitis virusNeuronal cellsNeuronsAlpha subunitCell linesStable transfectionStomatitis virusAxonsK-ATPaseIsoformsCellsDendrites
1987
Localization of Na+,K+-ATPase alpha-subunit to the sinusoidal and lateral but not canalicular membranes of rat hepatocytes.
Sztul ES, Biemesderfer D, Caplan MJ, Kashgarian M, Boyer JL. Localization of Na+,K+-ATPase alpha-subunit to the sinusoidal and lateral but not canalicular membranes of rat hepatocytes. Journal Of Cell Biology 1987, 104: 1239-1248. PMID: 3032985, PMCID: PMC2114466, DOI: 10.1083/jcb.104.5.1239.Peer-Reviewed Original ResearchConceptsAlpha-subunit bandsRat liver plasma membrane fractionsPlasma membraneAlpha subunitCatalytic activityMembrane fractionEntire plasma membranePlasma membrane fractionATPase alpha subunitIon-transporting epitheliaMonoclonal antibodiesWestern blotLiver plasma membrane fractionsBasolateral domainBasolateral distributionPolyclonal antibodies
1986
Newly synthesized Na,K-ATPase alpha-subunit has no cytosolic intermediate in MDCK cells.
Caplan MJ, Palade GE, Jamieson JD. Newly synthesized Na,K-ATPase alpha-subunit has no cytosolic intermediate in MDCK cells. Journal Of Biological Chemistry 1986, 261: 2860-2865. PMID: 3005269, DOI: 10.1016/s0021-9258(17)35866-0.Peer-Reviewed Original ResearchConceptsAlpha subunitAnimal cell plasma membranesK-ATPase alpha subunitMDCK cellsMembrane-bound vesiclesCell plasma membraneCytosol fractionTransmembrane proteinCrude cytosolic fractionPlasma membraneMembranous vesiclesPrecursor-product relationshipSoluble precursorsMembrane vesiclesK-ATPaseCytosolic fractionMembrane pelletVesiclesStaphylococcus aureus cellsAureus cellsCellsMonoclonal antibodiesProteinPrecursorsMembrane
1985
Molecular cloning of rat brain Na,K-ATPase alpha-subunit cDNA.
Schneider JW, Mercer RW, Caplan M, Emanuel JR, Sweadner KJ, Benz EJ, Levenson R. Molecular cloning of rat brain Na,K-ATPase alpha-subunit cDNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 6357-6361. PMID: 2994074, PMCID: PMC391053, DOI: 10.1073/pnas.82.18.6357.Peer-Reviewed Original ResearchConceptsRat brain NaBrain NaK-ATPase alpha subunitRat brainAlpha subunitCDNA clonesK-ATPase antibodiesCell linesFusion proteinCDNA insertK-ATPaseLambda gt11 cDNA expression libraryAlpha-subunit cDNACDNA fusion proteinDifferent rat tissuesK-ATPase polypeptidesTissue-specific patternsPositive phage clonesAmino acid sequenceAntibody reactiveCDNA expression libraryParental HeLa cellsMonoclonal antibodiesDog kidneyHuman cell lines