2011
Splice isoform estrogen receptors as integral transmembrane proteins
Kim KH, Toomre D, Bender JR. Splice isoform estrogen receptors as integral transmembrane proteins. Molecular Biology Of The Cell 2011, 22: 4415-4423. PMID: 21937726, PMCID: PMC3216666, DOI: 10.1091/mbc.e11-05-0416.Peer-Reviewed Original ResearchConceptsSplice isoformsTotal internal reflection fluorescence microscopySteroid hormone receptorsIntegral transmembrane proteinN-terminal ectodomainReflection fluorescence microscopyHormone receptorsTransmembrane proteinPlasma membraneProtein structureHuman endothelial cellsLigand engagementPotential novel therapeutic targetER46Fluorescence microscopyNovel therapeutic targetEcliptic pHluorinActivation signalsEndothelial nitric oxide synthase activationEstrogen receptor αENOS activationReceptor αIsoformsTherapeutic targetNitric oxide synthase activation
2009
Membrane-initiated actions of estrogen on the endothelium
Kim KH, Bender JR. Membrane-initiated actions of estrogen on the endothelium. Molecular And Cellular Endocrinology 2009, 308: 3-8. PMID: 19549586, PMCID: PMC2701909, DOI: 10.1016/j.mce.2009.03.025.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseNumerous signal transduction cascadesSignal transduction cascadeNitric oxideEndothelial cellsNon-genomic actionsAction of estrogenNitric oxide synthaseCaveolar membranesEstrogen receptor alphaTransduction cascadeC-SrcN-terminusShort isoformHuman endothelial cellsRapid activationProduct nitric oxideVascular studiesOxide synthaseReceptor alphaEstrogenVascular structuresER46Favorable effectCritical role
2007
Variant estrogen receptor–c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation
Li L, Hisamoto K, Kim KH, Haynes MP, Bauer PM, Sanjay A, Collinge M, Baron R, Sessa WC, Bender JR. Variant estrogen receptor–c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16468-16473. PMID: 17921256, PMCID: PMC2034248, DOI: 10.1073/pnas.0704315104.Peer-Reviewed Original ResearchConceptsC-SrcC-Src kinase activityTyrosine kinase c-SrcRapid signal transductionKinase c-SrcC-Src functionC-Src kinaseEndothelial NO synthase activationENOS activationMembrane recruitmentSignal transductionComplex assemblyPlasma membraneKinase activityOestrogen receptor-alpha variantsVenous endothelial cellsER46Pathway activationHormonal stimuliCritical roleArterial responseNO synthase activationSynthase activationStructural requirementsEndothelial cells
2003
Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
Li L, Haynes MP, Bender JR. Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 4807-4812. PMID: 12682286, PMCID: PMC153637, DOI: 10.1073/pnas.0831079100.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBase SequenceCell LineCell MembraneCOS CellsEndothelium, VascularEstrogen Receptor alphaGenes, ReporterGenetic VariationHumansNitric Oxide SynthaseNitric Oxide Synthase Type IIIProtein Processing, Post-TranslationalReceptors, EstrogenRecombinant ProteinsRNA, MessengerSubcellular FractionsTranscriptional ActivationTransfectionConceptsPlasma membranePalmitoylation-dependent mannerPlasma membrane localizationInhibition of palmitoylationFull-length ER alphaReporter gene transactivationCOS-7 cellsEndothelial cell proteinsMembrane localizationAlternative splicingEstrogen receptor α variantsOestrogen receptor-alpha variantsN-terminusHuman endothelial cellsCell proteinsER46Synthase pathwayAcid labelingHy926 cellsNonendothelial cellsENOS activationENOS phosphorylationCellsEndothelial cellsMembrane