2015
Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia
Alves DS, Thulin G, Loffing J, Kashgarian M, Caplan MJ. Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia. Journal Of The American Society Of Nephrology 2015, 26: 2765-2776. PMID: 25788531, PMCID: PMC4625659, DOI: 10.1681/asn.2013101040.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiotinylationCell LineCytoplasmDogsDynaminsEndocytosisEpithelial CellsGTPase-Activating ProteinsHumansIschemiaKidneyKidney DiseasesMadin Darby Canine Kidney CellsMaleMiceMice, KnockoutMicroscopy, FluorescencePhosphorylationProtein TransportReperfusion InjuryRNA, Small InterferingSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsRenal epithelial cellsATPase traffickingIntracellular compartmentsEpithelial cell polarityEpithelial cellsBasolateral plasma membraneGlucose transporter 4Cultured epithelial cellsCell polarityRab GTPaseAkt substratePlasma membraneSubcellular distributionAS160Energy depletionDirect bindingTransporter 4TraffickingDirect roleK-ATPaseATPaseTubular soluteIntracellular accumulationCellsCompartments
2009
Chapter 11 Detecting the Surface Localization and Cytoplasmic Cleavage of Membrane-Bound Proteins
Chapin HC, Rajendran V, Capasso A, Caplan MJ. Chapter 11 Detecting the Surface Localization and Cytoplasmic Cleavage of Membrane-Bound Proteins. Methods In Cell Biology 2009, 94: 223-239. PMID: 20362093, PMCID: PMC3063071, DOI: 10.1016/s0091-679x(08)94011-5.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Membrane-bound proteinsSubcellular localizationNuclear localizationPlasma membranePC1 proteinCytoplasmic cleavagePhysiological functionsSurface localizationFunctional roleSurface proteinsCell surfaceSurface populationsSpecific cleavageProteinImmunofluorescence protocolSoluble fragmentProtein expressionCell populationsImportant poolAutosomal dominant polycystic kidney diseasePolycystic kidney diseaseCleavageComplete understanding
2007
Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase
Kimura T, Allen PB, Nairn AC, Caplan MJ. Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase. Molecular Biology Of The Cell 2007, 18: 4508-4518. PMID: 17804821, PMCID: PMC2043564, DOI: 10.1091/mbc.e06-08-0711.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnimalsArrestinBinding, CompetitiveCell LineChlorocebus aethiopsChoroid PlexusCytoplasmG-Protein-Coupled Receptor KinasesKidneyMiceMicrofilament ProteinsNerve Tissue ProteinsPhosphorylationProtein BindingProtein SubunitsProtein TransportRabbitsSodium-Potassium-Exchanging ATPaseConceptsG protein-coupled receptorsLarge cytoplasmic loopExpression of spinophilinCytoplasmic loopMock-transfected cellsGRK-2Adrenergic hormonesReceptor signalingImportant modulatorSpinophilinATPase endocytosisATPase traffickingArrestin-2COS cellsArrestinHormoneAssociationATPaseGRKsCellsTraffickingEpsilonVasopressinReceptors
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membrane
2000
The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*
McCarthy J, Lim S, Elkind N, Trimmer J, Duvoisin R, Rodriguez-Boulan E, Caplan M. The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*. Journal Of Biological Chemistry 2000, 276: 9133-9140. PMID: 11106656, DOI: 10.1074/jbc.m008290200.Peer-Reviewed Original ResearchConceptsPolarized targetingCytoplasmic tailIntracellular compartmentsMadin-Darby canine kidney epithelial cellsVesicular stomatitis virus G proteinComplex neuronal functionMDCK cellsCell surface deliveryC-terminal tailCanine kidney epithelial cellsCytoplasmic tail domainVirus G proteinKidney epithelial cellsEntire cell surfaceCell surface expressionCytoplasmic domainTransmembrane portionSurface deliveryTail domainSynaptic microdomainsHuman placental alkaline phosphataseNeuronal polarizationMolecular signalsG proteinsCultured hippocampal neurons
1998
Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase.
Blostein R, Daly SE, Boxenbaum N, Lane LK, Arguello JM, Lingrel JB, Karlish SJ, Caplan MJ, Dunbar L. Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase. Acta Physiologica Scandinavica. Supplementum 1998, 643: 275-81. PMID: 9789570.Peer-Reviewed Original ResearchConceptsM2-M3 loopCytoplasmic domainCytoplasmic loopK-ATPaseN-terminusStructure/function analysisTransmembrane segment M2Amino-terminal halfMajor cytoplasmic loopFifth transmembrane segmentFirst cytoplasmic loopCatalytic phosphorylation siteMajor conformational statesLow catalytic turnoverPutative cationCytoplasmic mutantsTransmembrane segmentsPhosphorylation sitesTransmembrane domainAlpha 1 subunitSegment M2Cytoplasmic regionApparent affinityAmino terminusTerminal half