2002
The Spectrin-Ankyrin Skeleton Controls CD45 Surface Display and Interleukin-2 Production
Pradhan D, Morrow J. The Spectrin-Ankyrin Skeleton Controls CD45 Surface Display and Interleukin-2 Production. Immunity 2002, 17: 303-315. PMID: 12354383, DOI: 10.1016/s1074-7613(02)00396-5.Peer-Reviewed Original ResearchMeSH KeywordsAnkyrinsCD3 ComplexCell MembraneHumansInterleukin-2Jurkat CellsLeukocyte Common AntigensLymphocyte ActivationMacromolecular SubstancesMembrane GlycoproteinsNeoplasm ProteinsPeptide FragmentsProtein BindingProtein Interaction MappingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsSpectrinStructure-Activity RelationshipT-LymphocytesTransfectionConceptsJurkat T cellsT cell receptor stimulationCell receptor stimulationCytoplasmic domainSurface recruitmentBetaI spectrinSpectrin peptidesT cell activationSurface displayIntracellular poolUnexpected contributionAnkyrinSpectrinCell activationReceptor stimulationCD45T cellsCellsInterleukin-2 productionGlycoproteinRecruitmentT lymphocyte functionActivationLymphocyte functionPool
2001
βIII Spectrin Binds to the Arp1 Subunit of Dynactin*
Holleran E, Ligon L, Tokito M, Stankewich M, Morrow J, Holzbaur E. βIII Spectrin Binds to the Arp1 Subunit of Dynactin*. Journal Of Biological Chemistry 2001, 276: 36598-36605. PMID: 11461920, DOI: 10.1074/jbc.m104838200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBrainCell MembraneCOS CellsCytoplasmCytosolDynactin ComplexElectrophoresis, Polyacrylamide GelGlutathione TransferaseImmunoblottingImmunohistochemistryMicrofilament ProteinsMicrotubule-Associated ProteinsPrecipitin TestsProtein BindingProtein IsoformsProtein Structure, TertiaryRatsSpectrinSrc Homology DomainsTwo-Hybrid System TechniquesConceptsBetaIII spectrinGolgi vesicle traffickingMicrotubule motor complexAssociation of dyneinVesicle traffickingVesicular cargoRat brain cytosolMitotic spindleIntracellular motorsCytoplasmic dyneinCleavage furrowDynactinInterphase cellsArp1Spectrin isoformsCytoplasmic vesiclesF-actinActin bindsEndoplasmic reticulumPerinuclear regionNovel localizationSpectrinDyneinBrain cytosolΒIII spectrin[42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex
De Matteis M, Morrow J. [42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex. Methods In Enzymology 2001, 329: 405-416. PMID: 11210560, DOI: 10.1016/s0076-6879(01)29101-0.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAnimalsCell LineCell Membrane PermeabilityCoat Protein Complex IDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliFluorescent Antibody TechniqueGenetic VectorsGolgi ApparatusIntracellular MembranesPeptide FragmentsProtein BindingRecombinant Fusion ProteinsSpectrinConceptsADP-ribosylation factorGolgi membranesSpectrin peptidesPermeabilized cultured cellsBinding of spectrinCultured cell linesDifferent functional domainsSpectrin assemblySequence motifsRibosylation factorIndirect immunofluorescent microscopyFunctional domainsIntracellular distributionCultured cellsSpectrinΒIII spectrinImmunofluorescence analysisCell linesGolgiImmunofluorescent microscopyExperimental strategiesPeptidesMembraneCellsOrganelles
2000
α-Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo *
Pradhan D, Lombardo C, Roe S, Rimm D, Morrow J. α-Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo *. Journal Of Biological Chemistry 2000, 276: 4175-4181. PMID: 11069925, DOI: 10.1074/jbc.m009259200.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninAnimalsBinding SitesCell LineCell MembraneCytoskeletal ProteinsDogsHumansProtein BindingSpectrinConceptsInteraction of spectrinClone A cellsΑ-catenin bindsAmino-terminal domainAmino acid regionSpectrin-actin skeletonCell-cell contactCell adhesion processesMadin-Darby canine kidneyAdhesion complexesConfluent Madin Darby canine kidneyCytoskeletal assemblyPlasma membraneDetergent solubilityMembrane assemblyAcid regionSpectrin skeletonMembrane regionsA cellsVivo roleSpectrinPhospholipid interactionsBiological membranesE-cadherinMolecular interactionsIdentification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*
Wang Y, Morrow J. Identification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*. Journal Of Biological Chemistry 2000, 275: 8062-8071. PMID: 10713127, DOI: 10.1074/jbc.275.11.8062.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntibody SpecificityBlood ProteinsCloning, MolecularCytoskeletonDNA, ComplementaryErythrocyte MembraneHumansMembrane ProteinsMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsProtein BindingProtein BiosynthesisProtein Structure, TertiarySequence Analysis, DNASequence Analysis, ProteinSequence Homology, Amino AcidTissue DistributionConceptsIntegral membrane proteinsMembrane proteinsStomatin homologueSLP-1SLP-2Human stomatinCholesterol-rich lipid raftsLipid domain organizationTerminal hydrophobic domainAmino acid sequenceCultured COS cellsMature human erythrocytesSDS-polyacrylamide gel electrophoresis analysisErythrocyte membrane proteinsDomain organizationNonerythroid tissuesLipid raftsStomatin genePeripheral cytoskeletonChromosome 9p13StomatinAcid sequenceGel electrophoresis analysisCOS cellsRelated proteins
1998
ADP ribosylation factor regulates spectrin binding to the Golgi complex
Godi A, Santone I, Pertile P, Devarajan P, Stabach P, Morrow J, Di Tullio G, Polishchuk R, Petrucci T, Luini A, De Matteis M. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 8607-8612. PMID: 9671725, PMCID: PMC21123, DOI: 10.1073/pnas.95.15.8607.Peer-Reviewed Original ResearchConceptsADP-ribosylation factorGolgi complexRibosylation factorG proteinsVesicular stomatitis virus G proteinPleckstrin homology domainSmall G proteinsPH domain interactionBinding of spectrinVirus G proteinGolgi spectrinHomology domainPH domainCoat proteinDocking siteDomain interactionsGolgiEndoplasmic reticulumPtdInsP2 levelsDomain IPhospholipase DSpectrinGolgi fractionsProteinPtdInsP2
1994
Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.
Devarajan P, Scaramuzzino D, Morrow J. Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 2965-2969. PMID: 8159688, PMCID: PMC43495, DOI: 10.1073/pnas.91.8.2965.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitMembrane transport proteinsCytoplasmic domainAlpha subunitK-ATPaseTransport proteinsIntegral membrane transport proteinsDomain IIPutative cytoplasmic domainInteraction of ankyrinDistinct cytoplasmic domainsATPase domainHuman erythrocyte spectrinSignificant homologyUbiquitous proteinSpectrin cytoskeletonRecombinant fusion proteinPrimary sequenceAnkyrinFusion proteinChannel proteinsClear functionSubunitsProteinSpectrin binds
1992
Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells.
Fearon E, Finkel T, Gillison M, Kennedy S, Casella J, Tomaselli G, Morrow J, Van Dang C. Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 7958-7962. PMID: 1387709, PMCID: PMC49834, DOI: 10.1073/pnas.89.17.7958.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDNA-Binding ProteinsFlow CytometryFungal ProteinsHerpes Simplex Virus Protein Vmw65Hybrid CellsMacromolecular SubstancesMolecular Sequence DataProtein BindingRecombinant ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsTransfectionViral ProteinsConceptsProtein-protein interactionsMammalian cellsChimeric proteinReporter geneYeast transcriptional activator GAL4KISS systemSpecific protein-protein interactionsTranscriptional activator GAL4Transcriptional activation domainNovel protein interactionsDNA-binding domainTranscriptional activation functionSpecific interactionsActivator GAL4Activation domainProtein interactionsResultant transcriptionCDNA librarySelectable markerGAL4Drug resistance markersCell surfaceProteinTranscriptionGenes
1991
Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin.
Kennedy S, Warren S, Forget B, Morrow J. Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. Journal Of Cell Biology 1991, 115: 267-277. PMID: 1833409, PMCID: PMC2289929, DOI: 10.1083/jcb.115.1.267.Peer-Reviewed Original ResearchConceptsAmino-terminal halfRepeat unitsCarboxy-terminal halfCOOH-terminal thirdProkaryotic expression systemNonerythroid cellsIntegral proteinsErythrocyte membrane vesiclesBeta spectrinResidue segmentExpression systemAnkyrinNuclease digestionNonhomologous segmentsMembrane vesiclesTerminal thirdAttachment of spectrinNative spectrinSpectrinAmino acidsPosition 45RepeatsSedimentation velocity experimentsRepetitive unitsCDNAActin and tubulin binding domains of synapsins Ia and Ib.
Petrucci T, Morrow J. Actin and tubulin binding domains of synapsins Ia and Ib. Biochemistry 1991, 30: 413-22. PMID: 1899024, DOI: 10.1021/bi00216a016.Peer-Reviewed Original Research
1990
Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions
BECKER P, SCHWARTZ M, MORROW J, Samuel E. Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions. The FEBS Journal 1990, 193: 827-836. PMID: 2249696, DOI: 10.1111/j.1432-1033.1990.tb19406.x.Peer-Reviewed Original ResearchCalmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin.
Harris A, Morrow J. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 3009-3013. PMID: 2326262, PMCID: PMC53823, DOI: 10.1073/pnas.87.8.3009.Peer-Reviewed Original Research
1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Mische S, Mooseker M, Morrow J. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. Journal Of Cell Biology 1987, 105: 2837-2845. PMID: 3693401, PMCID: PMC2114693, DOI: 10.1083/jcb.105.6.2837.Peer-Reviewed Original ResearchAbnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding.
Becker P, Morrow J, Lux S. Abnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding. Journal Of Clinical Investigation 1987, 80: 557-565. PMID: 3611357, PMCID: PMC442269, DOI: 10.1172/jci113104.Peer-Reviewed Original ResearchBeta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
Coleman T, Harris A, Mische S, Mooseker M, Morrow J. Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions. Journal Of Cell Biology 1987, 104: 519-526. PMID: 3818791, PMCID: PMC2114562, DOI: 10.1083/jcb.104.3.519.Peer-Reviewed Original Research
1977
Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate.
Matthew J, Morrow J, Wittebort R, Gurd F. Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate. Journal Of Biological Chemistry 1977, 252: 2234-2244. PMID: 14958, DOI: 10.1016/s0021-9258(17)40546-1.Peer-Reviewed Original Research
1976
Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin.
Morrow J, Matthew J, Wittebort R, Gurd F. Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin. Journal Of Biological Chemistry 1976, 251: 477-484. PMID: 1395, DOI: 10.1016/s0021-9258(17)33904-2.Peer-Reviewed Original Research
1975
Nuclear Magnetic Resonance Studies Of Hemoglobin: Functional State Correlations And Isotopic Enrichment Strategie
Morrow J, Gurd F, Ho C. Nuclear Magnetic Resonance Studies Of Hemoglobin: Functional State Correlations And Isotopic Enrichment Strategie. Critical Reviews In Biochemistry 1975, 3: 221-287. PMID: 3388, DOI: 10.3109/10409237509105453.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsBinding SitesCarboxyhemoglobinHemeHemoglobinsHemoglobins, AbnormalHorsesHumansHydrogen-Ion ConcentrationIronMagnetic Resonance SpectroscopyMethemoglobinModels, MolecularMyoglobinOxyhemoglobinsProtein BindingProtein ConformationSpecies SpecificityWhales
1974
CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance
Morrow J, Keim P, Gurd F. CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance. Journal Of Biological Chemistry 1974, 249: 7484-7494. PMID: 4436319, DOI: 10.1016/s0021-9258(19)81264-4.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceAmino acidsProton nuclear magnetic resonanceDeuterium isotope effectChemical shiftsCO2 adductCertain amino acidsSperm whale myoglobinNMR measurementsMagnetic resonanceCarbon-13Fast exchangeMost amino acidsEquilibrium constantsCarbamino adductsIsotope effectWhale myoglobinStructural consequencesAdductsAcidPeptidesAccurate determinationNMRResonanceSensitive function13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2
Gurd F, Morrow J, Keim P, Visscher R, Marshall R. 13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2. Advances In Experimental Medicine And Biology 1974, 48: 109-124. PMID: 4215298, DOI: 10.1007/978-1-4684-0943-7_6.Peer-Reviewed Original ResearchConceptsMetal-protein interactionsInteraction of CO2NMR studiesHydrated derivativeNMR spectrometerSmall moleculesInteraction of HbCarbonate saltsBuffer componentsBicarbonate ionsCarbonic anhydraseCO2NMRUnquestionable importanceCommon strategySpeciesProteinIonsInsolubilityMoleculesSaltInteractionDerivativesBicarbonateSpectrometer