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
2002
Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane
Deen PM, Van Balkom BW, Savelkoul PJ, Kamsteeg EJ, Van Raak M, Jennings ML, Muth TR, Rajendran V, Caplan MJ. Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane. American Journal Of Physiology. Renal Physiology 2002, 282: f330-f340. PMID: 11788448, DOI: 10.1152/ajprenal.0168.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAquaporin 1Aquaporin 2Aquaporin 6AquaporinsArginine VasopressinBlood Group AntigensCell CompartmentationCell FractionationCell LineCell MembraneCell Membrane PermeabilityColforsinEndocytosisGene ExpressionHumansKidneyProtein Structure, TertiaryProtein TransportRatsRecombinant Fusion ProteinsVasoconstrictor AgentsWaterConceptsIntracellular vesiclesApical membraneAquaporin-2Wild‐type aquaporin‐2Mammalian water homeostasisMadin-Darby canine kidney cellsCanine kidney cellsAQP2 accumulationPrimary sequenceSame proteinOsmotic water permeabilityApical expressionForskolin treatmentAquaporin-1 (AQP1) water channelWater homeostasisKidney cellsBasolateral membraneVesiclesPlacental alkaline phosphataseMembraneWater channelsDuct cellsAQP1TailCells
1993
Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly
Gottardi CJ, Caplan MJ. Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly. Journal Of Biological Chemistry 1993, 268: 14342-14347. PMID: 8390991, DOI: 10.1016/s0021-9258(19)85246-8.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitK-ATPase beta subunitAlpha subunitBeta subunitCell surface expressionTerminal halfK-ATPaseCell surface deliveryEfficient cell surface expressionK-ATPase alphaNH2-terminal halfCOS-1 cellsIon-transporting ATPasesProtein domainsK-ATPase enzymeSubunit assemblySurface deliveryIntracellular vesiclesSubunit chimerasIndividual subunitsActive enzymeMolecular requirementsSubunitsCell surfaceBeta protein