2018
The Polycystin Complex Reveals Its Complexity
Padovano V, Caplan MJ. The Polycystin Complex Reveals Its Complexity. Biochemistry 2018, 57: 6917-6918. PMID: 30540438, DOI: 10.1021/acs.biochem.8b01205.Peer-Reviewed Original Research
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
Residues of the Fourth Transmembrane Segments of the Na,K-ATPase and the Gastric H,K-ATPase Contribute to Cation Selectivity*
Mense M, Dunbar L, Blostein R, Caplan M. Residues of the Fourth Transmembrane Segments of the Na,K-ATPase and the Gastric H,K-ATPase Contribute to Cation Selectivity*. Journal Of Biological Chemistry 2000, 275: 1749-1756. PMID: 10636871, DOI: 10.1074/jbc.275.3.1749.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsCationsElectrophysiologyH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationInhibitory Concentration 50KineticsMolecular Sequence DataMutationOuabainPotassiumRecombinant Fusion ProteinsSequence Homology, Amino AcidSodiumSodium-Potassium-Exchanging ATPaseStomachVanadatesXenopus laevisConceptsFourth transmembrane segmentTransmembrane segmentsATPase assaysK-ATPaseHelical wheel analysisTwo-electrode voltage-clamp experimentsCation selectivityProtein chimerasXenopus laevis oocytesVanadate sensitivityWild-type NaGastric HK-ATPasesXenopus oocytesLaevis oocytesATPase activityAbsence of sodiumResiduesTM4K counterpartsControl constructsOocytesConformational equilibriumAssaysImportant role
1997
Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry
Gu H, Caplan MJ, Rudnick G. Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry. Advances In Pharmacology 1997, 42: 175-179. PMID: 9327872, DOI: 10.1016/s1054-3589(08)60721-8.Peer-Reviewed Original ResearchMeSH KeywordsAmphetamineAnimalsBiological TransportCarrier ProteinsCell LineCell PolarityCloning, MolecularDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHumansKineticsMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsOrganic Anion TransportersRatsRecombinant Fusion ProteinsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSubstrate SpecificitySwineSymportersTransfectionConceptsCell linesPolarized epithelial cellsHeterologous expression systemBiogenic amine transportersCanine kidney cellsSame cellular backgroundKidney cell lineLLC-PK1 cellsExpression systemBiogenic amine releaseCellular backgroundIntact cellsPig kidney cell lineSame cDNAInhibitor sensitivityAmine transportersCatecholamine transportersCoupling stoichiometryTransportersKidney cellsDrug sensitivityPharmacological propertiesEpithelial cellsMolecule of substrateAmine release
1996
Real-time detection of the surface delivery of newly synthesized membrane proteins.
Andreose JS, Fumagalli G, Sigworth FJ, Caplan MJ. Real-time detection of the surface delivery of newly synthesized membrane proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 7661-7666. PMID: 8755532, PMCID: PMC38803, DOI: 10.1073/pnas.93.15.7661.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBungarotoxinsCell LineCell MembraneElectrophysiologyFourier AnalysisGolgi ApparatusGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateIon ChannelsKineticsMembrane PotentialsMembrane ProteinsMiceMuscle, SkeletalProtein Processing, Post-TranslationalReceptors, NicotinicTime FactorsConceptsMembrane proteinsPlasma membraneCell surfaceDegrees C temperature blockCultured muscle cellsConstitutive trafficTransport vesiclesConstitutive deliveryFusion eventsSurface deliveryFusion poreExocytotic vesiclesAChR moleculeGolgi complexTemperature blockAChR proteinNicotinic acetylcholine receptorsIon channel propertiesMost cellsVesiclesProteinCurrent fluctuationsMuscle cellsAcetylcholine receptorsGuanosine 5'
1993
Aldosterone-mediated Na/K-ATPase expression is alpha 1 isoform specific in the renal cortical collecting duct.
Welling PA, Caplan M, Sutters M, Giebisch G. Aldosterone-mediated Na/K-ATPase expression is alpha 1 isoform specific in the renal cortical collecting duct. Journal Of Biological Chemistry 1993, 268: 23469-23476. PMID: 8226873, DOI: 10.1016/s0021-9258(19)49486-6.Peer-Reviewed Original ResearchConceptsAlpha 1 formWestern blot analysisMineralocorticoid hormonesAlpha 1 isoformK-ATPase expressionAldosteroneAlpha-subunit isoformsK-ATPase moleculesNa/K-ATPase expressionK-ATPase catalytic subunitPump activityBlot analysisElectrophysiological assaysAlpha isoformAntipeptide antibodiesAttractive hypothesisDifferential regulationIsoform switchSubunit isoformsDuctNa/KIsoformsSodium affinityMolecular basisFunctional properties of an H,K-ATPase/Na,K-ATPase chimera
Blostein R, Zhang R, Gottardi C, Caplan M. Functional properties of an H,K-ATPase/Na,K-ATPase chimera. Journal Of Biological Chemistry 1993, 268: 10654-10658. PMID: 8387526, DOI: 10.1016/s0021-9258(18)82247-5.Peer-Reviewed Original Research
1990
Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery.
Caplan MJ, Forbush B, Palade GE, Jamieson JD. Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery. Journal Of Biological Chemistry 1990, 265: 3528-3534. PMID: 2154482, DOI: 10.1016/s0021-9258(19)39801-1.Peer-Reviewed Original Research
1986
Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes
Caplan M, Anderson H, Palade G, Jamieson J. Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes. Cell 1986, 46: 623-631. PMID: 3015421, DOI: 10.1016/0092-8674(86)90888-3.Peer-Reviewed Original ResearchConceptsBasolateral plasmalemmal domainsPlasmalemmal domainsNative proteinCell surface deliveryMadin-Darby canine kidney cellsBasolateral plasma membraneBasolateral cell surfacePulse labeling experimentsCanine kidney cellsIntracellular sortingProper sortingSurface deliveryPlasma membraneAcidic compartmentsDarby canine kidney cellsCell surfaceApical surfaceKidney cellsLabeling experimentsTwo-chamber culture systemProteinSortingCulture system