2015
Polycystin-1 Is a Cardiomyocyte Mechanosensor That Governs L-Type Ca2+ Channel Protein Stability
Pedrozo Z, Criollo A, Battiprolu PK, Morales CR, Contreras-Ferrat A, Fernández C, Jiang N, Luo X, Caplan MJ, Somlo S, Rothermel BA, Gillette TG, Lavandero S, Hill JA. Polycystin-1 Is a Cardiomyocyte Mechanosensor That Governs L-Type Ca2+ Channel Protein Stability. Circulation 2015, 131: 2131-2142. PMID: 25888683, PMCID: PMC4470854, DOI: 10.1161/circulationaha.114.013537.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornBiomarkersCalcium Channels, L-TypeCardiomegalyCells, CulturedFibrosisHypertrophyHypotonic SolutionsMaleMechanotransduction, CellularMiceMice, KnockoutMyocytes, CardiacProtein Interaction MappingProtein StabilityProtein Structure, TertiaryRatsRats, Sprague-DawleyRecombinant Fusion ProteinsRNA InterferenceStress, MechanicalTRPP Cation ChannelsConceptsL-type calcium channel activityCalcium channel activityNeonatal rat ventricular myocytesRat ventricular myocytesKnockout miceVentricular myocytesChannel activityMechanical stretchNeonatal rat ventricular myocyte hypertrophyProtein levelsVentricular myocyte hypertrophyL-type Ca2G protein-coupled receptor-like proteinPolycystin-1Channel protein levelsCyclic mechanical stretchControl miceInterstitial fibrosisStress-induced activationCardiac massMechanical stress-induced activationCardiac functionRNAi-dependent knockdownCardiac hypertrophyLittermate controls
2009
POSH Stimulates the Ubiquitination and the Clathrin-independent Endocytosis of ROMK1 Channels*
Lin DH, Yue P, Pan CY, Sun P, Zhang X, Han Z, Roos M, Caplan M, Giebisch G, Wang WH. POSH Stimulates the Ubiquitination and the Clathrin-independent Endocytosis of ROMK1 Channels*. Journal Of Biological Chemistry 2009, 284: 29614-29624. PMID: 19710010, PMCID: PMC2785594, DOI: 10.1074/jbc.m109.041582.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBiological TransportCell LineClathrinDynaminsEpithelial Sodium ChannelsGene Expression RegulationHumansKidney Tubules, CollectingOocytesPotassium Channels, Inwardly RectifyingProtein Sorting SignalsProtein Structure, TertiaryRatsRats, Sprague-DawleyUbiquitinationUbiquitin-Protein LigasesXenopus laevisConceptsHEK293T cellsClathrin-independent endocytosisE3 ubiquitin ligaseUbiquitin ligaseGlutathione S-transferase pulldown experimentsROMK1 channelsT cellsTyrosine-based internalization signalPotassium currentROMK channelsDominant-negative dynaminImmunoprecipitation of lysatesInternalization signalInhibitory effectPulldown experimentsScaffold proteinUbiquitination assaysRING domainUbiquitinationN-terminusGamma subunitsAmino acidsENaC-alphaROMK1Tissue lysates
2008
Expression of Tetraspan Protein CD63 Activates Protein-tyrosine Kinase (PTK) and Enhances the PTK-induced Inhibition of ROMK Channels*
Lin D, Kamsteeg EJ, Zhang Y, Jin Y, Sterling H, Yue P, Roos M, Duffield A, Spencer J, Caplan M, Wang WH. Expression of Tetraspan Protein CD63 Activates Protein-tyrosine Kinase (PTK) and Enhances the PTK-induced Inhibition of ROMK Channels*. Journal Of Biological Chemistry 2008, 283: 7674-7681. PMID: 18211905, DOI: 10.1074/jbc.m705574200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBenzoquinonesCSK Tyrosine-Protein KinaseEnzyme InhibitorsFemaleGene Expression RegulationHumansKidney CortexKidney MedullaLactams, MacrocyclicMaleOocytesOrgan SpecificityPatch-Clamp TechniquesPhosphorylationPlatelet Membrane GlycoproteinsPotassium Channels, Inwardly RectifyingProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsRats, Sprague-DawleyReceptor-Like Protein Tyrosine Phosphatases, Class 4RifabutinSrc-Family KinasesTetraspanin 30TransfectionXenopus laevisConceptsExpression of CD63T cellsOuter medullaRenal cortexROMK channelsProtein tyrosine kinasesC-SrcRole of CD63Potassium restrictionROMK activityPotassium currentTwo-electrode voltage clampRat kidneyDecreased expressionImmunocytochemical stainingROMK1 channelsInhibitory effectMedullaNative rat kidneyCD63Voltage clampCortexRPTPalphaTyrosine phosphorylationHerbimycin A
2003
The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit
Duffield A, Kamsteeg EJ, Brown AN, Pagel P, Caplan MJ. The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 15560-15565. PMID: 14660791, PMCID: PMC307607, DOI: 10.1073/pnas.2536699100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDChlorocebus aethiopsCloning, MolecularCOS CellsGene LibraryH(+)-K(+)-Exchanging ATPaseHumansKidneyMembrane ProteinsModels, BiologicalPlatelet Membrane GlycoproteinsProtein SubunitsProtein TransportRabbitsRatsRats, Sprague-DawleyRecombinant ProteinsTetraspanin 30TransfectionConceptsAdaptor protein complex 2Intracellular compartmentsK-ATPaseTetraspanin CD63K-ATPase β-subunitCOS-7 cellsEndocytic machineryAdaptor proteinLate endosomesSecretory vesiclesPlasma membraneGastric parietal cellsBiochemical experimentsInteraction partnersΒ-subunitParietal cellsCell surfaceEnhanced endocytosisTubulovesicular elementsCD63CompartmentsCellsInternalizationComplexes 2Endosomes
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
1995
Na+,K+-ATPase in the Choroid Plexus REGULATION BY SEROTONIN/PROTEIN KINASE C PATHWAY (∗)
Fryckstedt J, Caplan M, Aperia A, Fisone G, Snyder G, Greengard P. Na+,K+-ATPase in the Choroid Plexus REGULATION BY SEROTONIN/PROTEIN KINASE C PATHWAY (∗). Journal Of Biological Chemistry 1995, 270: 2427-2430. PMID: 7852300, DOI: 10.1074/jbc.270.6.2427.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChoroid PlexusMalePhorbol 12,13-DibutyratePhosphorylationProtein Kinase CRatsRats, Sprague-DawleySerotoninSodium-Potassium-Exchanging ATPaseConceptsProtein kinase CKinase CTwo-dimensional peptide mappingProtein kinase C pathwayKinase C pathwayProtein phosphorylationFirst messengersIntact cellsIon pumpsPeptide mappingATPaseC pathwayPhosphorylationPhorbolDemonstrated abilityMessengerComigrationActivatorRegulationPathwayActivityChoroid plexusMechanismProductionTurnover