2013
Olfactory receptor responding to gut microbiota-derived signals plays a role in renin secretion and blood pressure regulation
Pluznick JL, Protzko RJ, Gevorgyan H, Peterlin Z, Sipos A, Han J, Brunet I, Wan LX, Rey F, Wang T, Firestein SJ, Yanagisawa M, Gordon JI, Eichmann A, Peti-Peterdi J, Caplan MJ. Olfactory receptor responding to gut microbiota-derived signals plays a role in renin secretion and blood pressure regulation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 4410-4415. PMID: 23401498, PMCID: PMC3600440, DOI: 10.1073/pnas.1215927110.Peer-Reviewed Original ResearchConceptsShort-chain fatty acidsRenin secretionBlood pressureGut microbiotaG protein-coupled receptor 41Acute hypotensive responseRenal juxtaglomerular apparatusSmall resistance vesselsMicrobiota-derived signalsModulate blood pressureBlood pressure regulationWild-type miceSmooth muscle cellsG protein-coupled receptorsGPR41 expressionOlfactory receptorsHypotensive responseProtein-coupled receptorsSCFA receptorsResistance vesselsJuxtaglomerular apparatusAntibiotic treatmentOlfr78Receptor 41Knockout miceActivation of the Ca2+-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane
Jouret F, Wu J, Hull M, Rajendran V, Mayr B, Schöfl C, Geibel J, Caplan MJ. Activation of the Ca2+-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane. Journal Of Cell Science 2013, 126: 5132-5142. PMID: 24013548, PMCID: PMC3828589, DOI: 10.1242/jcs.127555.Peer-Reviewed Original ResearchConceptsTJ assemblyMDCK cellsStable transfectionFunction mutant formZO-1Tight junction components ZO-1G protein-coupled receptorsHuman CaSRCell-cell contactEpithelial cell plasma membranesMadin-Darby canine kidney cellsCell plasma membraneStimulation of CaSRDivalent ion homeostasisCanine kidney cellsTight junctionsJunction-associated proteinsTight junction componentsEndogenous CaSRProtein kinasePlasma membraneIon homeostasisMutant formsChelator BAPTA-AMCell differentiation
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