2024
Ezrin drives adaptation of monocytes to the inflamed lung microenvironment
Gudneppanavar R, Di Pietro C, H Öz H, Zhang P, Cheng E, Huang P, Tebaldi T, Biancon G, Halene S, Hoppe A, Kim C, Gonzalez A, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. Cell Death & Disease 2024, 15: 864. PMID: 39613751, PMCID: PMC11607083, DOI: 10.1038/s41419-024-07255-8.Peer-Reviewed Original ResearchConceptsActivation of focal adhesion kinaseExtracellular matrixActin-binding proteinsFocal adhesion kinaseLung extracellular matrixKnock-out mouse modelProtein kinase signalingCortical cytoskeletonLoss of ezrinKinase signalingPlasma membraneCell migrationSignaling pathwayEzrinResponse to lipopolysaccharideTissue-resident macrophagesMouse modelLipopolysaccharideCytoskeletonEzrin expressionLung microenvironmentKinaseMonocyte recruitmentProteinAktEzrin drives adaptation of monocytes to the inflamed lung microenvironment.
Gudneppanavar R, Di Pietro C, Oez H, Zhang P, Huang P, Braga C, Tebaldi T, Biancon G, Kim C, Gonzalez A, Halene S, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. The Journal Of Immunology 2024, 212: 0078_5418-0078_5418. DOI: 10.4049/jimmunol.212.supp.0078.5418.Peer-Reviewed Original ResearchRNA-seqActin-binding protein ezrinF-actin distributionImmune response to bacteriaCystic fibrosisIn vitro functional studiesResponse to bacteriaIncreased expression of pro-inflammatory markersCytoskeleton rearrangementF-actinResponse to lung infectionExpressed genesProtein ezrinTranscriptional profilesExpression of pro-inflammatory markersPlasma membranePro-inflammatory markersFunctional studiesEzrinLung extracellular matrixCF miceExtracellular matrixWT micePI3K/Akt signalingLung infection
2021
The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration
Rahimi N, Ho R, Chandler K, De La Cena K, Amraei R, Mitchel A, Engblom N, Costello C. The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration. Journal Of Biomedical Science 2021, 28: 61. PMID: 34503512, PMCID: PMC8427838, DOI: 10.1186/s12929-021-00757-z.Peer-Reviewed Original ResearchConceptsMitotic spindle organizationERM familyΑ-tubulinSpindle organizationCell migrationApical localizationN-terminal ERM domainCRISPR/Cas9-mediated knockoutMitotic spindle assemblyCell-cell adhesionCas9-mediated knockoutFilopodia-like protrusionsNovel tumor suppressorComplex functional interplayActin organizationERM domainLysine acetylationTMIGD1Spindle assemblyCarboxyl terminusFunctional interplayMoesinCell cycleTumor suppressorEzrin
2017
Ezrin links CFTR to TLR4 signaling to orchestrate anti-bacterial immune response in macrophages
Di Pietro C, Zhang PX, O’Rourke T, Murray TS, Wang L, Britto CJ, Koff JL, Krause DS, Egan ME, Bruscia EM. Ezrin links CFTR to TLR4 signaling to orchestrate anti-bacterial immune response in macrophages. Scientific Reports 2017, 7: 10882. PMID: 28883468, PMCID: PMC5589856, DOI: 10.1038/s41598-017-11012-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorCytoskeletal ProteinsDisease Models, AnimalMacrophage ActivationMacrophagesMicePhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktPseudomonas aeruginosaPseudomonas InfectionsSignal TransductionToll-Like Receptor 4ConceptsCystic fibrosis transmembrane conductance regulatorPI3K/AktFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorPI3K/Akt signalingConductance regulatorAnti-bacterial immune responseAkt signalingAltered localizationEzrinCystic fibrosis diseaseMφ activationAktProtein levelsFibrosis diseaseActivationImmune regulationPhagocytosisInductionDirect linkSignalingRegulatorImmune responseMΦMacrophages
2013
Ezrin Is Required for the Functional Regulation of the Epithelial Sodium Proton Exchanger, NHE3
Hayashi H, Tamura A, Krishnan D, Tsukita S, Suzuki Y, Kocinsky HS, Aronson PS, Orlowski J, Grinstein S, Alexander RT. Ezrin Is Required for the Functional Regulation of the Epithelial Sodium Proton Exchanger, NHE3. PLOS ONE 2013, 8: e55623. PMID: 23405179, PMCID: PMC3566197, DOI: 10.1371/journal.pone.0055623.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonAnimalsColonCyclic AMPCytoskeletal ProteinsDogsEpithelial CellsFluorescence Recovery After PhotobleachingHumansMadin Darby Canine Kidney CellsMaleMembrane ProteinsMiceMice, KnockoutMicrofilament ProteinsMicrovilliOctoxynolPhosphorylationProtein TransportRNA, Small InterferingSodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersConceptsApical actin cytoskeletonNHE3 activitySodium hydrogen exchanger isoform 3CAMP-dependent inhibitionEzrin knockdown miceERM proteinsActin cytoskeletonSodium-proton exchangerApical cytoskeletonApical localizationFunctional regulationWild-type animalsEpithelial cell culture modelEzrinProton exchangersFluorescent recoveryEpithelial phenotypeCytoskeletonMolecular determinantsCell culture modelExchanger isoform 3Functional studiesNon-targeting siRNAApical membraneIsoform 3
2007
Proteomic Analysis of the Resistance to Aplidin in Human Cancer Cells
González-Santiago L, Alfonso P, Suárez Y, Núñez A, García-Fernández LF, Alvarez E, Muñoz A, Casal JI. Proteomic Analysis of the Resistance to Aplidin in Human Cancer Cells. Journal Of Proteome Research 2007, 6: 1286-1294. PMID: 17338558, DOI: 10.1021/pr060430+.Peer-Reviewed Original ResearchConceptsProtein disulfide isomeraseRole of PDINumber of proteinsRab geranylgeranyltransferaseInduction of apoptosisHuman cancer cellsDisulfide isomeraseProteomic approachMembrane proteinsProteomic analysisMALDI-TOF mass spectrometryApoptosis pathwayDatabase interrogationHeLa cellsCyclophilin AProteinCancer cellsAplidinApoptosisCystathionine gamma lyaseCellsMass spectrometryGeranylgeranyltransferaseEzrinIsomerase
2006
Expression of ezrin in glial tubes in the adult subventricular zone and rostral migratory stream
Cleary MA, Uboha N, Picciotto MR, Beech RD. Expression of ezrin in glial tubes in the adult subventricular zone and rostral migratory stream. Neuroscience 2006, 143: 851-861. PMID: 16996217, PMCID: PMC1712626, DOI: 10.1016/j.neuroscience.2006.08.028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsbeta CateninBlotting, WesternBromodeoxyuridineCell MovementCell ProliferationCerebral VentriclesCytoskeletal ProteinsEfferent PathwaysGene ExpressionGlial Fibrillary Acidic ProteinImmunohistochemistryMiceNerve Growth FactorsNeural Cell Adhesion Molecule L1NeurogliaS100 Calcium Binding Protein beta SubunitS100 ProteinsSialic AcidsTubulinConceptsRostral migratory streamTube cellsCell-matrix recognitionExpression of ezrinCell type-specific markersCell-cell interactionsNeural cell adhesion molecule 1Specific cell typesStem cell proliferationSubventricular zoneBi-directional signalsMigratory streamERM proteinsERM familyCellular functionsEarly neuronal markerSignal transductionAdult subventricular zoneCell motilityEzrinCell typesGlial tubesCell membraneNeuronal migrationPrecursor cells
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