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
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
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
Functional 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