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
2007
MAL decreases the internalization of the aquaporin-2 water channel
Kamsteeg EJ, Duffield AS, Konings IB, Spencer J, Pagel P, Deen PM, Caplan MJ. MAL decreases the internalization of the aquaporin-2 water channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16696-16701. PMID: 17940053, PMCID: PMC2034241, DOI: 10.1073/pnas.0708023104.Peer-Reviewed Original ResearchConceptsAquaporin-2 water channelIntracellular vesiclesApical membrane proteinsMembrane-associated proteinsTrafficking of AQP2Apical surface expressionEpithelial cellsCell surface retentionApical plasma membraneInvolvement of MALBody water homeostasisS256 phosphorylationWater channel proteinsSurface expressionApical deliveryRegulated traffickingSorting eventsRenal epithelial cellsMembrane associationMembrane proteinsPosttranslational modificationsProtein interactionsPlasma membraneChannel proteinsWater channels
1999
Nongastric H+,K+-ATPase: cell biologic and functional properties.
Grishin AV, Reinhard J, Dunbar LA, Courtois-Coutry N, Wang T, Giebisch G, Caplan MJ. Nongastric H+,K+-ATPase: cell biologic and functional properties. Seminars In Nephrology 1999, 19: 421-30. PMID: 10511382.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedH(+)-K(+)-Exchanging ATPaseHumansIon TransportKidney Tubules, CollectingMiceMice, TransgenicStomachUrotheliumWater-Electrolyte BalanceConceptsATPase isoformsP-type ATPasesEndocytic regulationEndocytosis signalATPase familyCell machineryCytoplasmic tailK resorptionATPasesIon pumpsATPase isoform expressionApical surfaceIsoformsCell biologicIsoform expressionPhysiological studiesTubule epithelial cellsATPaseEpithelial cellsTransgenic miceCation transportK transportFunctional propertiesRenal K transportEndocytosis
1998
A tyrosine-based signal regulates H-K-ATPase-mediated potassium reabsorption in the kidney
Wang T, Courtois-Coutry N, Giebisch G, Caplan M. A tyrosine-based signal regulates H-K-ATPase-mediated potassium reabsorption in the kidney. American Journal Of Physiology 1998, 275: f818-f826. PMID: 9815140, DOI: 10.1152/ajprenal.1998.275.5.f818.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsH(+)-K(+)-Exchanging ATPaseKidney Tubules, CollectingMaleMiceMice, Inbred C57BLMice, TransgenicPotassiumSignal TransductionTyrosineConceptsGlomerular filtration rateTransgenic miceGastric acid outputPlasma K concentrationK pumpK-ATPaseRenal collecting tubulesK clearanceBlood pressurePotassium reabsorptionAcid outputUrine volumeK excretionFiltration rateGastric acidK reabsorptionPump functionCollecting tubuleMicePlasma NaTyrosine-based sequenceTyrosine-based signalsKidneyExcretionCytoplasmic tail
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 ResearchMeSH KeywordsAldosteroneAnimalsBlotting, WesternFemaleIsoenzymesKidney Tubules, CollectingKineticsOuabainRabbitsSodium-Potassium-Exchanging ATPaseConceptsAlpha 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 basis