2019
Everything You Always Wanted to Know about β3-AR * (* But Were Afraid to Ask)
Schena G, Caplan MJ. Everything You Always Wanted to Know about β3-AR * (* But Were Afraid to Ask). Cells 2019, 8: 357. PMID: 30995798, PMCID: PMC6523418, DOI: 10.3390/cells8040357.Peer-Reviewed Original ResearchConceptsNovel pharmacological approachesCurrent clinical practiceNovel therapeutic targetAR signalingΒ3-ARPharmacological approachesOcular diseasesTherapeutic targetAdrenergic receptorsClinical practiceFindings translateClinical areasCellular modelSuitable animalAppealing targetInter-species differencesDiseaseReceptors
2012
Novel sensory signaling systems in the kidney
Pluznick JL, Caplan MJ. Novel sensory signaling systems in the kidney. Current Opinion In Nephrology & Hypertension 2012, 21: 404-409. PMID: 22569342, DOI: 10.1097/mnh.0b013e328354a6bd.Peer-Reviewed Original Research
2009
Dystroglycan and AMP Kinase: Polarity's Protectors when the Power Goes Out
Zhang L, Seo-Mayer P, Caplan MJ. Dystroglycan and AMP Kinase: Polarity's Protectors when the Power Goes Out. Developmental Cell 2009, 16: 1-2. PMID: 19154710, PMCID: PMC2997531, DOI: 10.1016/j.devcel.2008.12.004.Peer-Reviewed Original Research
2007
Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase
Kimura T, Allen PB, Nairn AC, Caplan MJ. Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase. Molecular Biology Of The Cell 2007, 18: 4508-4518. PMID: 17804821, PMCID: PMC2043564, DOI: 10.1091/mbc.e06-08-0711.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnimalsArrestinBinding, CompetitiveCell LineChlorocebus aethiopsChoroid PlexusCytoplasmG-Protein-Coupled Receptor KinasesKidneyMiceMicrofilament ProteinsNerve Tissue ProteinsPhosphorylationProtein BindingProtein SubunitsProtein TransportRabbitsSodium-Potassium-Exchanging ATPaseConceptsG protein-coupled receptorsLarge cytoplasmic loopExpression of spinophilinCytoplasmic loopMock-transfected cellsGRK-2Adrenergic hormonesReceptor signalingImportant modulatorSpinophilinATPase endocytosisATPase traffickingArrestin-2COS cellsArrestinHormoneAssociationATPaseGRKsCellsTraffickingEpsilonVasopressinReceptors
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membrane