Biff Forbush, PhD
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Cellular & Molecular Physiology
PO Box 208026, 333 Cedar Street
New Haven, CT 06520-8026
United States
About
Titles
Professor Emeritus of Cellular And Molecular Physiology
Appointments
Cellular & Molecular Physiology
EmeritusPrimary
Other Departments & Organizations
Education & Training
- PhD
- Johns Hopkins University (1975)
Research
Overview
Medical Subject Headings (MeSH)
Membrane Proteins; Muscle Cells; Physiology; Sodium-Potassium-Chloride Symporters
Research at a Glance
Yale Co-Authors
Frequent collaborators of Biff Forbush's published research.
Publications Timeline
A big-picture view of Biff Forbush's research output by year.
Research Interests
Research topics Biff Forbush is interested in exploring.
Dianqing (Dan) Wu, PhD
Jesse Rinehart, PhD
Michael Caplan, PhD, MD
Patrick Gallagher, MD, BS
8Publications
459Citations
Sodium-Potassium-Chloride Symporters
Membrane Proteins
Publications
2012
Regulatory activation is accompanied by movements in the Cterminus of the Na‐K‐Cl cotransporter (NKCC1)
Monette M, Forbush B. Regulatory activation is accompanied by movements in the Cterminus of the Na‐K‐Cl cotransporter (NKCC1). The FASEB Journal 2012, 26: 604.3-604.3. DOI: 10.1096/fasebj.26.1_supplement.604.3.Peer-Reviewed Original ResearchCitationsConceptsC-terminusFluorescence resonance energy transferNa-K-Cl cotransporterRegulatory activationTransporter activationFRET decreasesSame C-terminusKey structural roleEmbryonic kidney cell lineYellow fluorescent proteinHuman embryonic kidney cell lineRegulation of NKCC1Phosphatase inhibitorCalyculin A.Kidney cell linePlasma membraneN-terminusFluorescent proteinStructural roleTransport activityResonance energy transferCell typesHEK cellsFunction of NKCC1Regulatory processes
2011
Functional Analysis of Transmembrane Domain 3 in NKCC1
Somasekharan S, Forbush B. Functional Analysis of Transmembrane Domain 3 in NKCC1. Biophysical Journal 2011, 100: 245a-246a. DOI: 10.1016/j.bpj.2010.12.1558.Peer-Reviewed Original Research
2009
Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity
Rinehart J, Maksimova Y, Tanis J, Stone K, Hodson C, Zhang J, Risinger M, Pan W, Wu D, Colangelo C, Forbush B, Joiner C, Gulcicek E, Gallagher P, Lifton R. Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity. Journal Of End-to-End-testing 2009, 138: 525-536. DOI: 10.1016/s9999-9994(09)20441-7.Peer-Reviewed Original ResearchConceptsIntrinsic transport activityK-Cl cotransporterTransport activityCell volume regulationRegulated phosphorylationRNA interferenceAlanine substitutionsCultured cellsHomologous sitesKCC activityWNK1 expressionNeonatal mouse brainVolume regulationNeuronal functionHypotonic conditionsActive cotransportPhosphorylationIntracellular chloride concentrationCotransporter activityKCC3Human red blood cellsKCC2 activationFundamental roleMouse brainRegulation
2008
Apical membrane expression of NKCC2 is directed by a domain within its cytoplasmic C‐terminus
Carmosino M, Gimenez I, Caplan M, Forbush B. Apical membrane expression of NKCC2 is directed by a domain within its cytoplasmic C‐terminus. The FASEB Journal 2008, 22: 935.4-935.4. DOI: 10.1096/fasebj.22.1_supplement.935.4.Peer-Reviewed Original ResearchConceptsC-terminusNa-K-Cl cotransporterMolecular basisRenal Na-K-Cl cotransporterMDCK cellsCytoplasmic C-terminusTransient expression analysisApical membrane expressionRenal epithelial cell lineBasolateral traffickingResidue stretchEpithelial cell lineApical localizationExpression analysisCentral playerMammalian kidneyApical expressionApical membraneMembrane expressionCorresponding regionLimb cellsCell linesBasolateral membraneThick ascending limb cellsNKCC2
2006
The Residues Determining Differences in Ion Affinities among the Alternative Splice Variants F, A, and B of the Mammalian Renal Na-K-Cl Cotransporter (NKCC2)*
Giménez I, Forbush B. The Residues Determining Differences in Ion Affinities among the Alternative Splice Variants F, A, and B of the Mammalian Renal Na-K-Cl Cotransporter (NKCC2)*. Journal Of Biological Chemistry 2006, 282: 6540-6547. PMID: 17186942, DOI: 10.1074/jbc.m610780200.Peer-Reviewed Original ResearchCitationsMeSH Keywords and Concepts
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 ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH 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
2001
Ion transport and ligand binding by the Na–K–Cl cotransporter, structure–function studies
Isenring P, Forbush B. Ion transport and ligand binding by the Na–K–Cl cotransporter, structure–function studies. Comparative Biochemistry And Physiology Part A Molecular & Integrative Physiology 2001, 130: 487-497. PMID: 11913460, DOI: 10.1016/s1095-6433(01)00420-2.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsNa-K-Cl cotransporterK-Cl cotransporterCation-Cl(-) cotransportersC-terminusStructure-function studiesGroups of residuesTransmembrane segmentsMutational approachAnimal cellsCentral domainVariant residuesLigand bindingIon transportDistinct carriersNa-Cl cotransporterResiduesSpecies differencesCotransporterBindingLoop diureticsAnion transportAvailable sulfhydryl groupsSulfhydryl groupsMovement of NaDifferent substratesModulation 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 ResearchCitationsMeSH Keywords and ConceptsConceptsProtein 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
Links & Media
News
- January 09, 2020
Cellular and Molecular Physiology Annual Retreat 2019
- December 06, 2018
Cellular and Molecular Physiology Annual Retreat 2018
- October 02, 2017
Cellular and Molecular Physiology Annual Retreat 2017
- October 04, 2016
Cellular and Molecular Physiology Annual Retreat 2016
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Cellular & Molecular Physiology
PO Box 208026, 333 Cedar Street
New Haven, CT 06520-8026
United States