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 recruitmentProteinAkt
1998
Polarization of the Na+, K+-ATPase in Epithelia Derived from the Neuroepithelium
Rizzolo L. Polarization of the Na+, K+-ATPase in Epithelia Derived from the Neuroepithelium. International Review Of Cytology 1998, 185: 195-235. PMID: 9750268, DOI: 10.1016/s0074-7696(08)60152-7.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsProper membrane domainDifferent sorting signalsPolarity mechanismsSorting signalsMembrane domainsMembrane proteinsCortical cytoskeletonCertain environmental stimuliFascinating groupMaintenance signalsApical membraneEnvironmental stimuliIon pumpsProteinBasolateral membraneATPaseYields insightsNeuroepitheliumMembraneCellsCytoskeletonEpitheliumRetinal pigment epitheliumSignalsPigment epithelium
1995
The distribution of Na+,K+-atpase and 5a11 antigen in apical microvilli of the retinal pigment epithelium is unrelated to α-spectrin
Rizzolo L, Zhou S. The distribution of Na+,K+-atpase and 5a11 antigen in apical microvilli of the retinal pigment epithelium is unrelated to α-spectrin. Journal Of Cell Science 1995, 108: 3623-3633. PMID: 8586673, DOI: 10.1242/jcs.108.11.3623.Peer-Reviewed Original ResearchConceptsAlpha-spectrinPlasma membranePlasma membrane proteinsDevelopment of polarityLateral plasma membraneBasal plasma membraneMembrane proteinsCortical cytoskeletonMacromolecular complexesBeta spectrinAnkyrinChick embryogenesisApical poleCytoskeletonEmbryonic day 6RPE microvilliLateral membranesReceptor proteinMost epitheliaSpectrin distributionΑ-spectrinApical membraneIon pumpsApical microvilliProtein
1993
Calmodulin-binding domain of recombinant erythrocyte beta-adducin.
Scaramuzzino D, Morrow J. Calmodulin-binding domain of recombinant erythrocyte beta-adducin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3398-3402. PMID: 8475088, PMCID: PMC46307, DOI: 10.1073/pnas.90.8.3398.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesBlood ProteinsCalmodulinCalmodulin-Binding ProteinsCalpainCattleCloning, MolecularDNAErythrocytesKineticsMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesPhosphorylationProtein Structure, SecondaryRecombinant ProteinsRestriction MappingTrypsinConceptsCaM-binding activityBeta-adducinBundles F-actinProtease-sensitive domainsCAMP-dependent kinaseCaM-binding domainPartial cDNA cloneBinding of spectrinAmino acid codeDependent CaM bindingProtein kinase CSingle letter amino acid codeCaM-binding sequenceProtease-resistant corePEST sequenceCovalent phosphorylationShares structural featuresCDNA clonesCortical cytoskeletonHeterodimeric proteinStructural basisConsensus sequenceMammalian erythrocytesProtease sensitivityBind calmodulin
1989
Calmodulin Regulates Fodrin Susceptibility to Cleavage by Calciumdependent Protease I
Harris A, Croall D, Morrow J. Calmodulin Regulates Fodrin Susceptibility to Cleavage by Calciumdependent Protease I. Journal Of Biological Chemistry 1989, 264: 17401-17408. PMID: 2551900, DOI: 10.1016/s0021-9258(18)71508-1.Peer-Reviewed Original ResearchConceptsAlpha subunitProtease IAbsence of CaMRegulated proteolysisEukaryotic cellsRegulation of plasticityCortical cytoskeletonCalmodulin bindingQuaternary structureBeta subunitSubunitsTetrameric formCalcium-dependent proteolysisFodrinProteolysisCaM antagonistsAlpha-fodrinFunctional evidenceDifferential susceptibilityCaM.Fodrin proteolysisIsotonic bufferCytoskeletonClose proximityCalmodulinAnkyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.
Morrow J, Cianci C, Ardito T, Mann A, Kashgarian M. Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. Journal Of Cell Biology 1989, 108: 455-465. PMID: 2537316, PMCID: PMC2115445, DOI: 10.1083/jcb.108.2.455.Peer-Reviewed Original ResearchConceptsMadin-Darby canine kidney cellsCanine kidney cellsK-ATPaseAlpha subunitMolecular mechanismsMDCK cellsMinor membrane proteinsDistribution of fodrinErythrocyte ankyrinConfluent MDCK cellsBinding of ankyrinKidney cellsHuman erythrocyte ankyrinRenal epithelial cellsCytoplasmic domainNonerythroid cellsMembrane proteinsCortical cytoskeletonBasolateral domainMembrane skeletonPolarized distributionAnkyrinBasolateral marginsCell developmentErythrocyte band 3
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