2021
The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2
Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. Communications Biology 2021, 4: 226. PMID: 33597714, PMCID: PMC7889885, DOI: 10.1038/s42003-021-01750-w.Peer-Reviewed Original ResearchConceptsCryo-electron microscopy structureHuman NKCC1Microscopy structureEssential residuesFunctional characterizationKCC transportersPlasma membraneStructural basisTransepithelial saltTransport activityMechanistic understandingTransportersStructural studiesCritical roleCotransporter NKCC1Computational analysisIon transportWater transportNeuronal excitabilityNKCC1PhosphorylationCell volumeNKCCKCC2Residues
2003
PASK (Proline-Alanine-rich STE20-related Kinase), a Regulatory Kinase of the Na-K-Cl Cotransporter (NKCC1)*
Dowd BF, Forbush B. PASK (Proline-Alanine-rich STE20-related Kinase), a Regulatory Kinase of the Na-K-Cl Cotransporter (NKCC1)*. Journal Of Biological Chemistry 2003, 278: 27347-27353. PMID: 12740379, DOI: 10.1074/jbc.m301899200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineDNA, ComplementaryDose-Response Relationship, DrugGenes, DominantGenetic VectorsHumansMarine ToxinsOxazolesOxidative StressPhosphorylationPrecipitin TestsProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryRatsRubidiumSharksSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 2ThreonineTime FactorsConceptsNa-K-Cl cotransporterN-terminal regulatory domainPhosphorylation-dependent activationHEK cellsInhibitor calyculin ANKCC1 activityRegulatory domainCoimmunoprecipitation assaysRegulatory kinasesActivation of NKCC1Calyculin ARegulated eventNKCC1 activationPhosphorylationKinaseSharksCotransporter activityOverexpressionCotransporter expressionNKCC1CellsActivationBindingCotransporterMutants
1991
[3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins
Haas M, Dunham P, Forbush B. [3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins. American Journal Of Physiology 1991, 260: c791-c804. PMID: 2018111, DOI: 10.1152/ajpcell.1991.260.4.c791.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAnimalsBenzophenonesBumetanideCarcinoma, Ehrlich TumorCarrier ProteinsCell FractionationCell MembraneCentrifugation, Density GradientFemaleKidneyKidney CortexKidney MedullaKineticsMembrane ProteinsMiceProtein BindingSodium-Potassium-Chloride SymportersSulfanilamidesTritiumConceptsMouse kidney membranesKidney membranesNa-K-Cl cotransport systemNa-K-ClLow-affinity peakDog kidney membraneMouse Ehrlich ascites tumor cellsMouse kidney proteinsDog kidneyCrude plasma membranesTumor cellsWestern blot analysisEhrlich ascites tumor cellsCotransport systemAscites tumor cellsMouse kidneyMiceStaining profileLow-affinity sitesWestern blottingBinding sitesAntiserum cross-reactedKidneyBlot analysisKidney proteins
1990
Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery.
Caplan MJ, Forbush B, Palade GE, Jamieson JD. Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery. Journal Of Biological Chemistry 1990, 265: 3528-3534. PMID: 2154482, DOI: 10.1016/s0021-9258(19)39801-1.Peer-Reviewed Original Research
1988
Overview: occluded ions and Na, K-ATPase.
Forbush B. Overview: occluded ions and Na, K-ATPase. Progress In Clinical And Biological Research 1988, 268A: 229-48. PMID: 2843866.Peer-Reviewed Original Research
1984
Na+ movement in a single turnover of the Na pump.
Forbush B. Na+ movement in a single turnover of the Na pump. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 5310-5314. PMID: 6089192, PMCID: PMC391693, DOI: 10.1073/pnas.81.17.5310.Peer-Reviewed Original Research
1982
Purification and characterization of an (Na++K+)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain
Collins J, Forbush B, Lane L, Ling E, Schwartz A, Zot A. Purification and characterization of an (Na++K+)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain. Biochimica Et Biophysica Acta 1982, 686: 7-12. PMID: 6279154, DOI: 10.1016/0005-2736(82)90145-6.Peer-Reviewed Original Research
1979
Direct photoaffinity labeling of the primary region of the ouabain binding site of (Na+ + K+)-ATPase with [3H]ouabain, [3H]digitoxin and [3H]digitoxigenin
Forbush B, Hoffman J. Direct photoaffinity labeling of the primary region of the ouabain binding site of (Na+ + K+)-ATPase with [3H]ouabain, [3H]digitoxin and [3H]digitoxigenin. Biochimica Et Biophysica Acta 1979, 555: 299-306. PMID: 224926, DOI: 10.1016/0005-2736(79)90169-x.Peer-Reviewed Original ResearchEvidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated from Pi.
Forbush B, Hoffman J. Evidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated from Pi. Biochemistry 1979, 18: 2308-15. PMID: 221003, DOI: 10.1021/bi00578a027.Peer-Reviewed Original Research
1978
Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase.
Forbush B, Kaplan J, Hoffman J. Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase. Biochemistry 1978, 17: 3667-76. PMID: 210802, DOI: 10.1021/bi00610a037.Peer-Reviewed Original Research