2013
Polycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease.
Bertuccio CA, Caplan MJ. Polycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease. Medicina 2013, 73: 155-62. PMID: 23570767.Peer-Reviewed Original ResearchConceptsPolycystin-1Polycystin-2Autosomal dominant polycystic kidney diseaseTerminal cytoplasmic tailProtein sortingNormal tubulogenesisPolycystic kidney diseaseProtein functionCytoplasmic tailTerminal tailCommon genetic causeCystogenic processExtracellular matrixDifferentiation mechanismsCellular proliferationGenetic causeMultiple cleavagesDominant polycystic kidney diseasePathwayHigh proliferative rateCleavageProliferative rateSecretory characteristicsGenesTubulogenesis
2008
The Cytoplasmic Tail Dileucine Motif LL572 Determines the Glycosylation Pattern of Membrane-type 1 Matrix Metalloproteinase*
Ludwig T, Theissen SM, Morton MJ, Caplan MJ. The Cytoplasmic Tail Dileucine Motif LL572 Determines the Glycosylation Pattern of Membrane-type 1 Matrix Metalloproteinase*. Journal Of Biological Chemistry 2008, 283: 35410-35418. PMID: 18955496, PMCID: PMC2602891, DOI: 10.1074/jbc.m801816200.Peer-Reviewed Original ResearchConceptsMT1-MMPMT1-MMP traffickingSite-directed mutagenesis studiesCell surface traffickingMembrane type 1 matrix metalloproteinasePost-translational processingCytoplasmic tailMolecular charactersMutagenesis studiesSurface traffickingMetabolic labelingSubstrate spectrumMatrix metalloproteinaseEnzymatic deglycosylationGlycosylation patternsProfound physiological effectsHinge regionTraffickingPathological processesProteinLectin precipitationPost-synthetic pathwayPhysiological effectsMajor effectBroad spectrum
2004
Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis
Nguyen NV, Gleeson PA, Courtois-Coutry N, Caplan MJ, van Driel IR. Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis. Gastroenterology 2004, 127: 145-154. PMID: 15236181, DOI: 10.1053/j.gastro.2004.04.016.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneIntracellular traffickingTyrosine-based endocytosis motifATPase activityATPase beta subunitMembrane traffickingATPase endocytosisTrafficking eventsEndocytosis motifParietal cell ultrastructureTubulovesicular compartmentCytoplasmic tailIntracytoplasmic compartmentCl- conductanceParietal cell acid secretionBeta subunitParietal cellsDirect regulationProton pumpCell ultrastructureTraffickingATPaseCellsRegulation
2000
The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*
McCarthy J, Lim S, Elkind N, Trimmer J, Duvoisin R, Rodriguez-Boulan E, Caplan M. The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*. Journal Of Biological Chemistry 2000, 276: 9133-9140. PMID: 11106656, DOI: 10.1074/jbc.m008290200.Peer-Reviewed Original ResearchConceptsPolarized targetingCytoplasmic tailIntracellular compartmentsMadin-Darby canine kidney epithelial cellsVesicular stomatitis virus G proteinComplex neuronal functionMDCK cellsCell surface deliveryC-terminal tailCanine kidney epithelial cellsCytoplasmic tail domainVirus G proteinKidney epithelial cellsEntire cell surfaceCell surface expressionCytoplasmic domainTransmembrane portionSurface deliveryTail domainSynaptic microdomainsHuman placental alkaline phosphataseNeuronal polarizationMolecular signalsG proteinsCultured hippocampal neurons
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 ResearchConceptsATPase 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 ResearchConceptsGlomerular 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 tailIdentification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*
Muth T, Ahn J, Caplan M. Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*. Journal Of Biological Chemistry 1998, 273: 25616-25627. PMID: 9748227, DOI: 10.1074/jbc.273.40.25616.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCells, CulturedCloning, MolecularDogsFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidGenes, mycIon ChannelsKidneyMembrane ProteinsMembrane Transport ProteinsMicroscopy, ConfocalMolecular Sequence DataRecombinant Fusion ProteinsSequence DeletionConceptsC-terminal cytoplasmic tailIon transport proteinsMadin-Darby canine kidney cellsCytoplasmic tailMembrane proteinsC-terminusCanine kidney cellsTransporter familyAmino acidsBasolateral distributionTransport proteinsGAT-2Polytopic membrane proteinsProtein-based signalsProtein-protein interactionsTerminal cytoplasmic tailC-terminal sequencesKidney cellsClass of polypeptidesEpithelial cellsApical sortingPDZ domainChimeric transportersPolarized sortingSorting determinantTyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*
Roush D, Gottardi C, Naim H, Roth M, Caplan M. Tyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*. Journal Of Biological Chemistry 1998, 273: 26862-26869. PMID: 9756932, DOI: 10.1074/jbc.273.41.26862.Peer-Reviewed Original ResearchConceptsProtein sorting signalsTyrosine-based motifLLC-PK1 cellsCytoplasmic tailSorting signalsMDCK cellsApical membraneBeta-subunit polypeptidesBasolateral membraneK-ATPase beta subunitDi-leucine motifBeta subunit proteinLLC-PK1 epithelial cellsMadin-Darby canine kidney cellsMadin-Darby canine kidneyEpithelial cell typesCanine kidney cellsK-ATPase betaHA-Y543Cytoplasmic sequencesSequence motifsSubunit polypeptidesMembrane proteinsBasolateral domainPolarized epitheliumSorting of P-type ATPases in polarized epithelial cells.
Dunbar LA, Courtois-Coutry N, Roush DL, Muth TR, Gottardi CJ, Rajendran V, Geibel J, Kashgarian M, Caplan MJ. Sorting of P-type ATPases in polarized epithelial cells. Acta Physiologica Scandinavica. Supplementum 1998, 643: 289-95. PMID: 9789572.Peer-Reviewed Original ResearchConceptsApical localizationK-ATPaseMost epithelial cell typesTyrosine-based signalsP-type familyP-type ATPasesEpithelial cellsCritical tyrosine residuesApical plasma membraneFourth transmembrane domainBeta-subunit sequencesApical cell surfaceEpithelial cell typesSorting signalsTransmembrane domainCytoplasmic tailSequence domainsPlasma membraneHomologous membersTyrosine residuesParietal cellsStorage compartmentCell typesCell surfaceBasolateral surface
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 secretionReinternalizationPlasmalemma