2005
The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit
Zatti A, Chauvet V, Rajendran V, Kimura T, Pagel P, Caplan MJ. The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit. Molecular Biology Of The Cell 2005, 16: 5087-5093. PMID: 16107561, PMCID: PMC1266409, DOI: 10.1091/mbc.e05-03-0200.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Cytoplasmic C-terminal tailK-ATPase α-subunitPolycystin-1 proteinK-ATPase activityRegulation of NaChinese hamster ovary cellsProtein interactsHamster ovary cellsProtein exhibitΑ-subunitFunctional studiesAmino acidsPKD1 geneOvary cellsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseasePolycystic kidney diseaseInteractsKinetic propertiesRegulationGenesTailProtein
2000
A 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 proteinsResidues 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
1999
Cation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras*
Blostein R, Dunbar L, Mense M, Scanzano R, Wilczynska A, Caplan M. Cation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras*. Journal Of Biological Chemistry 1999, 274: 18374-18381. PMID: 10373442, DOI: 10.1074/jbc.274.26.18374.Peer-Reviewed Original Research
1998
ATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump*
Grishin A, Caplan M. ATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump*. Journal Of Biological Chemistry 1998, 273: 27772-27778. PMID: 9774385, DOI: 10.1074/jbc.273.43.27772.Peer-Reviewed Original Research
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 systemEvidence for a high and specific concentration of (Na+,K+)ATPase in the plasma membrane of the osteoclast
Baron R, Neff L, Roy C, Boisvert A, Caplan M. Evidence for a high and specific concentration of (Na+,K+)ATPase in the plasma membrane of the osteoclast. Cell 1986, 46: 311-320. PMID: 2424614, DOI: 10.1016/0092-8674(86)90748-8.Peer-Reviewed Original ResearchConceptsPlasma membraneOsteoclast plasma membraneBone resorptionBeta subunitProton translocationMonoclonal antibodiesImmunoblot analysisBone marrow cellsKidney tubule cellsExtracellular compartmentBone marrow preparationsMembraneMarrow cellsBone cellsTubule cellsCellsProton transportOsteoclast membraneMarrow preparationsIon transportOsteoclastsSodium pumpSpecific markersResorptionAntibodies