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
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 interactionsDevelopment and characterization of antibodies specific to caspase-3-produced alpha II-spectrin 120 kDa breakdown product: marker for neuronal apoptosis
Nath R, Huggins M, Glantz S, Morrow J, McGinnis K, Nadimpalli R, Wang K. Development and characterization of antibodies specific to caspase-3-produced alpha II-spectrin 120 kDa breakdown product: marker for neuronal apoptosis. Neurochemistry International 2000, 37: 351-361. PMID: 10825575, DOI: 10.1016/s0197-0186(00)00040-1.Peer-Reviewed Original ResearchConceptsWestern blotRat cerebellar granule neuronsHuman neuroblastoma SH-SY5Y cellsNeuroblastoma SH-SY5Y cellsSpectrin breakdown productsCerebellar granule neuronsSH-SY5Y cellsApoptotic neuronsCharacterization of antibodiesNeuronal apoptosisNeurodegenerative conditionsGranule neuronsBreakdown productsImmunocytochemical studySH-SY5YII-spectrinWithdrawal-induced apoptosisAntibodiesNeuronsCaspase-3Apoptotic deathPowerful markerChicken antibodiesApoptosisAlpha-spectrin
1997
α-Catenin Can Form Asymmetric Homodimeric Complexes and/or Heterodimeric Complexes with ॆ-Catenin*
Koslov E, Maupin P, Pradhan D, Morrow J, Rimm D. α-Catenin Can Form Asymmetric Homodimeric Complexes and/or Heterodimeric Complexes with ॆ-Catenin*. Journal Of Biological Chemistry 1997, 272: 27301-27306. PMID: 9341178, DOI: 10.1074/jbc.272.43.27301.Peer-Reviewed Original ResearchConceptsMembrane adhesion complexesHomodimeric complexCadherin moleculesAdhesion complexesAdhesive complexesHeterodimeric complexΑ-cateninOligomeric stateSurface plasmon resonance assaysMultimeric stateResidues 54Relative stoichiometryBiophysical techniquesMolecular massCell adhesionAmino acidsRecombinant moleculesHuman alphaRotary shadowingResonance assaysPrecise stoichiometryComplexesCytoskeletonCateninHomodimerSite-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin
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 bindsA partial structural repeat forms the heterodimer self-association site of all beta-spectrins
Kennedy S, Weed S, Forget B, Morrow J. A partial structural repeat forms the heterodimer self-association site of all beta-spectrins. Journal Of Biological Chemistry 1994, 269: 11400-11408. PMID: 8157672, DOI: 10.1016/s0021-9258(19)78138-1.Peer-Reviewed Original ResearchAmino Acid SequenceBase SequenceBinding SitesCloning, MolecularDNA PrimersErythrocytesEscherichia coliGlutathione TransferaseHumansKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataProtein Structure, SecondaryRecombinant Fusion ProteinsRecombinant ProteinsRepetitive Sequences, Nucleic AcidSpectrin
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
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 Research
1988
The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site.
Harris A, Croall D, Morrow J. The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site. Journal Of Biological Chemistry 1988, 263: 15754-15761. PMID: 2844821, DOI: 10.1016/s0021-9258(19)37652-5.Peer-Reviewed Original Research
1986
A calmodulin and α-subunit binding domain in human erythrocyte spectrin
Sears D, Marchesi V, Morrow J. A calmodulin and α-subunit binding domain in human erythrocyte spectrin. Biochimica Et Biophysica Acta 1986, 870: 432-442. PMID: 3697360, DOI: 10.1016/0167-4838(86)90251-7.Peer-Reviewed Original ResearchConceptsCalmodulin binding siteSpectrin-actin membrane skeletonBinding sitesSubunit-subunit associationMr fragmentTwo-dimensional peptide mappingPutative calmodulin binding siteErythrocyte spectrinNon-erythroid spectrinCleavage of spectrinHuman erythrocyte spectrinProtein 4.1Cyanogen bromide cleavageMembrane skeletonActin bindingCalmodulin bindingNH2 terminusBind calmodulinNative conditionsBeta subunitCalmodulin regulationTerminal regionSpectrinPeptide mappingCalmodulinMechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin
Harris A, Anderson J, Yurchenco P, Green L, Ainger K, Morrow J. Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin. Journal Of Cellular Biochemistry 1986, 30: 51-69. PMID: 2420811, DOI: 10.1002/jcb.240300107.Peer-Reviewed Original Research
1980
Identification of functional domains of human erythrocyte spectrin.
Morrow J, Speicher D, Knowles W, Hsu C, Marchesi V. Identification of functional domains of human erythrocyte spectrin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 6592-6596. PMID: 6935670, PMCID: PMC350332, DOI: 10.1073/pnas.77.11.6592.Peer-Reviewed Original ResearchConceptsHuman erythrocyte spectrinErythrocyte membrane vesiclesMembrane vesiclesBinding of spectrinErythrocyte spectrinHigh-affinity membraneCleavage of spectrinFunctional domainsCytoplasmic surfaceDimeric spectrinProtein receptorsPolypeptide chainTerminal regionSpectrinTemperature-dependent associationUnique polypeptide chainsNoncovalent associationTerminal portionAlpha chainBeta chain
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 function