2007
The Future of the Pump
Caplan MJ. The Future of the Pump. Journal Of Clinical Gastroenterology 2007, 41: s217-s222. PMID: 17575526, DOI: 10.1097/mcg.0b013e31803233da.Peer-Reviewed Original ResearchConceptsIon transport proteinsLarge macromolecular complexesMacromolecular complexesGastric parietal cellsTransport proteinsSecond messengerMacromolecular interactionsIon translocationRegulatory processesK-ATPaseCritical roleTight controlX-ray crystallographic techniquesParietal cellsCrystallographic techniquesCellsKinasePharmacologic suppressionTraffickingProteinTranslocationMessengerMolecular structureRegulationSecretion
2003
Ion Pump‐Interacting Proteins: Promising New Partners
PAGEL P, ZATTI A, KIMURA T, DUFFIELD A, CHAUVET V, RAJENDRAN V, CAPLAN MJ. Ion Pump‐Interacting Proteins: Promising New Partners. Annals Of The New York Academy Of Sciences 2003, 986: 360-368. PMID: 12763851, DOI: 10.1111/j.1749-6632.2003.tb07215.x.Peer-Reviewed Original Research
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
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 ResearchMeSH KeywordsAmino Acid SubstitutionCytoplasmIsoenzymesMutationProtein ConformationSodium-Potassium-Exchanging ATPaseConceptsM2-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 halfA basolateral sorting signal is encoded in the α-subunit of Na-K-ATPase
Muth TR, Gottardi CJ, Roush DL, Caplan MJ. A basolateral sorting signal is encoded in the α-subunit of Na-K-ATPase. American Journal Of Physiology 1998, 274: c688-c696. PMID: 9530100, DOI: 10.1152/ajpcell.1998.274.3.c688.Peer-Reviewed Original ResearchConceptsLLC-PK1 cellsK-ATPaseAmino acidsPlasma membrane distributionIntracellular vesicular compartmentsBasolateral surfaceAmino acid residuesNa-K-ATPaseBasolateral signalSurface expressionK-ATPase sequencesProtein domainsPlasma membraneVesicular compartmentsGastric parietal cellsTranscriptional upregulationΑ-subunitLLC-PK1 cell lineMembrane distributionAcid residuesSecretagogue stimulationIon pumpsApical surfaceChimerasCell lines