2003
Short-term Stimulation of the Renal Na-K-Cl Cotransporter (NKCC2) by Vasopressin Involves Phosphorylation and Membrane Translocation of the Protein*
Giménez I, Forbush B. Short-term Stimulation of the Renal Na-K-Cl Cotransporter (NKCC2) by Vasopressin Involves Phosphorylation and Membrane Translocation of the Protein*. Journal Of Biological Chemistry 2003, 278: 26946-26951. PMID: 12732642, DOI: 10.1074/jbc.m303435200.Peer-Reviewed Original ResearchConceptsNa-K-Cl cotransporterRenal Na-K-Cl cotransporterCell membrane compartmentsRegulatory threonineMembrane compartmentsAntidiuretic hormone vasopressinPhosphospecific antibodiesMembrane translocationAmino terminusCytoplasmic vesiclesNKCC2 phosphorylationShort-term activationApical membranePhosphorylationTerm activationHormone vasopressinShort-term stimulationThick ascending limbProteinTranslocationCotransporterNKCC2ActivationAscending limbMorphometric analysis
2002
A Regulatory Locus of Phosphorylation in the N Terminus of the Na-K-Cl Cotransporter, NKCC1*
Darman RB, Forbush B. A Regulatory Locus of Phosphorylation in the N Terminus of the Na-K-Cl Cotransporter, NKCC1*. Journal Of Biological Chemistry 2002, 277: 37542-37550. PMID: 12145304, DOI: 10.1074/jbc.m206293200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineDogfishHumansIon TransportKineticsModels, MolecularPeptide FragmentsPhosphopeptidesPhosphorylationProtein ConformationRecombinant ProteinsSalt GlandSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 2Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTransfectionTrypsinConceptsProtein phosphatase 1 bindsN-terminusSer/ThrPhosphorylation-dependent mechanismN-terminal domainStrong consensus siteNa-K-Cl cotransporter NKCC1Matrix-assisted laser desorption ionization timePhosphoregulatory mechanismsPhosphoacceptor sitesRegulatory lociHEK-293 cellsNa-K-Cl cotransporterLaser desorption ionization timeCalyculin AConsensus sitesPhosphorylation stoichiometryDesorption ionization timeAmino acidsTryptic fragmentsProteinGland tubulesRectal gland tubulesFlight mass spectrometryIonization time
2001
Modulation of Ion Transport by Direct Targeting of Protein Phosphatase Type 1 to the Na-K-Cl Cotransporter*
Darman R, Flemmer A, Forbush B. Modulation of Ion Transport by Direct Targeting of Protein Phosphatase Type 1 to the Na-K-Cl Cotransporter*. Journal Of Biological Chemistry 2001, 276: 34359-34362. PMID: 11466303, DOI: 10.1074/jbc.c100368200.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Substrate proteinsNa-K-Cl cotransporterProtein phosphatase type 1Phosphatase type 1Intracellular chloride regulationPhosphatase specificityRegulatory phosphorylationPhosphatase 1Catalytic subunitMotif bindsSubunit bindsN-terminusPP1cMajor proteinsDirect bindingDirect interactionChloride regulationProteinGeneral mechanismDirect targetingMutantsMotifSubunitsBinds
2000
Basolateral K-Cl Cotransporter Regulates Colonic Potassium Absorption in Potassium Depletion*
Sangan P, Brill S, Sangan S, Forbush B, Binder H. Basolateral K-Cl Cotransporter Regulates Colonic Potassium Absorption in Potassium Depletion*. Journal Of Biological Chemistry 2000, 275: 30813-30816. PMID: 10878016, DOI: 10.1074/jbc.m003931200.Peer-Reviewed Original ResearchConceptsK-Cl cotransporterMembrane HK-Cl cotransportActive potassium absorptionProtein expressionBasolateral membranePotassium absorptionK-ATPaseNorthern blot analysisKCC1 mRNACoordinated regulationAlpha-subunit mRNABeta-subunit mRNAMRNA abundanceBlot analysisMRNAExpressionProteinMembraneCotransporterDepletionRat distal colonCDNAKCC1
1988
Photoaffinity labelling of a 150 kDa (Na + K + Cl)-cotransport protein from duck red cells with an analog of bumetanide
Haas M, Forbush B. Photoaffinity labelling of a 150 kDa (Na + K + Cl)-cotransport protein from duck red cells with an analog of bumetanide. Biochimica Et Biophysica Acta 1988, 939: 131-144. PMID: 3349075, DOI: 10.1016/0005-2736(88)90054-5.Peer-Reviewed Original ResearchConceptsDuck red cellsRed cellsSimultaneous presence of Na+Binding to intact cellsIncubation mediumDog kidney membraneConsistent with labelingDuck red blood cellsRed blood cellsBumetanideCotransporterRed cell membraneBlood cellsKidney membranesPresence of Na+DucksCellsCell membranePlasma membraneSDS-polyacrylamide gelsIntact cellsSDS-polyacrylamideProteinNorepinephrine
1983
Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin
Forbush B. Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin. Analytical Biochemistry 1983, 128: 159-163. PMID: 6303151, DOI: 10.1016/0003-2697(83)90356-1.Peer-Reviewed Original ResearchConceptsMaximal Na,K-ATPase activityAmount of membrane proteinNa,K-ATPase activityElectric organ of eelIsolated plasma membranesNa,K-ATPaseSodium dodecyl sulfate bufferK-ATPase activityPlasma membrane preparationsTransmembrane proteinsMembrane proteinsDetergent bufferPlasma membraneOptimal activityActivity of membranesBovine serum albuminMembrane vesiclesK-ATPasePermeability of membrane vesiclesDetergentDetergent activitySulfate bufferProteinVesicular natureSerum albumin