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
2000
The cell biology of ion pumps: sorting and regulation
Dunbar L, Caplan M. The cell biology of ion pumps: sorting and regulation. European Journal Of Cell Biology 2000, 79: 557-563. PMID: 11001492, DOI: 10.1078/0171-9335-00079.Peer-Reviewed Original ResearchConceptsP-type familyPolarized epithelial cellsIon pumpsK-ATPaseDistinct regulatory pathwaysProtein traffickingSubcellular localizationCell biologyRelated membersRegulatory pathwaysMolecular signalsCellular mechanismsEnzymatic activityIntra-molecular interactionsEpithelial cellsTraffickingComplex arrayCatalytic capacityPhysiologic functionATPasesHomologyBiologyPathwayRegulationSortingThe Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*
Asano S, Kawada K, Kimura T, Grishin A, Caplan M, Takeguchi N. The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*. Journal Of Biological Chemistry 2000, 275: 8324-8330. PMID: 10722662, DOI: 10.1074/jbc.275.12.8324.Peer-Reviewed Original ResearchConceptsAlpha/beta assemblyN-glycosylation sitesATPase activityBeta assemblyPutative N-glycosylation sitesCarbohydrate chainsAlpha/beta complexSingle carbohydrate chainCatalytic subunitSurface deliveryFunctional enzymeAsparagine residuesAlpha subunitΒ-subunitBeta complexDelivery mechanismFunctional expressionComplete lossATPaseAssemblyExpressionSubunits
1997
A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion
Courtois-Coutry N, Roush D, Rajendran V, McCarthy J, Geibel J, Kashgarian M, Caplan M. A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion. Cell 1997, 90: 501-510. PMID: 9267030, DOI: 10.1016/s0092-8674(00)80510-3.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCOS CellsCytomegalovirusDNA PrimersEndocytosisGastric AcidGastric MucosaH(+)-K(+)-Exchanging ATPaseMacromolecular SubstancesMiceMice, TransgenicMicroscopy, ImmunoelectronMutagenesis, Site-DirectedParietal Cells, GastricPolymerase Chain ReactionPromoter Regions, GeneticRecombinant ProteinsSignal TransductionTransfectionTyrosineConceptsK-ATPase beta subunitTyrosine-based signalsK-ATPaseTyrosine-based endocytosis signalTyrosine residuesBeta subunitIntracellular storage compartmentEndocytosis signalCytoplasmic tailMutant betaRegulated compartmentsSecrete acidResidue sequenceStorage compartmentCell surfaceCell plasmalemmaSubunitsTransgenic miceParietal cellsGastric glandsCompartmentsSecretionAcid secretionReinternalizationPlasmalemmaIon pumps in epithelial cells: sorting, stabilization, and polarity
Caplan MJ. Ion pumps in epithelial cells: sorting, stabilization, and polarity. American Journal Of Physiology 1997, 272: g1304-g1313. PMID: 9227464, DOI: 10.1152/ajpgi.1997.272.6.g1304.Peer-Reviewed Original Research
1994
Sorting of the Gastric H,K‐ATPase in Endocrine and Epithelial Cellsa
ROUSH D, GOTTARDI C, CAPLAN M. Sorting of the Gastric H,K‐ATPase in Endocrine and Epithelial Cellsa. Annals Of The New York Academy Of Sciences 1994, 733: 212-222. PMID: 7978870, DOI: 10.1111/j.1749-6632.1994.tb17271.x.Peer-Reviewed Original Research
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