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
1997
Site-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
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 ResearchMeSH KeywordsAnimalsCalmodulinCalpainCarrier ProteinsCattleElectrophoresis, Polyacrylamide GelKineticsMacromolecular SubstancesMicrofilament ProteinsMolecular WeightOsmolar ConcentrationSulfonamidesConceptsAlpha subunitProtease IAbsence of CaMRegulated proteolysisEukaryotic cellsRegulation of plasticityCortical cytoskeletonCalmodulin bindingQuaternary structureBeta subunitSubunitsTetrameric formCalcium-dependent proteolysisFodrinProteolysisCaM antagonistsAlpha-fodrinFunctional evidenceDifferential susceptibilityCaM.Fodrin proteolysisIsotonic bufferCytoskeletonClose proximityCalmodulin
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
Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinases
Croall D, Morrow J, DeMartino G. Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinases. Biochimica Et Biophysica Acta 1986, 882: 287-296. PMID: 3015225, DOI: 10.1016/0304-4165(86)90250-3.Peer-Reviewed Original ResearchMeSH KeywordsAnion Exchange Protein 1, ErythrocyteBlood ProteinsCalcimycinCalpainCytoskeletal ProteinsElectrophoresis, Polyacrylamide GelErythrocyte MembraneHumansLeupeptinsMembrane ProteinsMersalylNeuropeptidesSpectrinA 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 ResearchMeSH KeywordsBinding SitesCalmodulinChromatography, AffinityElectrophoresis, Polyacrylamide GelErythrocyte MembraneHumansMacromolecular SubstancesMolecular WeightPeptide FragmentsSpectrinTrypsinConceptsCalmodulin 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 mappingCalmodulin
1985
Mechanism of cytoskeletal regulation (I): functional differences correlate with antigenic dissimilarity in human brain and erythrocyte spectrin
Harris A, Green L, Ainger K, Morrow J. Mechanism of cytoskeletal regulation (I): functional differences correlate with antigenic dissimilarity in human brain and erythrocyte spectrin. Biochimica Et Biophysica Acta 1985, 830: 147-158. PMID: 2410030, DOI: 10.1016/0167-4838(85)90022-6.Peer-Reviewed Original ResearchMeSH KeywordsBrain ChemistryCross ReactionsElectrophoresis, Polyacrylamide GelEpitopesErythrocytesHumansImmunosorbent TechniquesMicroscopy, ElectronMolecular WeightPolymersSpectrin
1983
[23] Erythrocyte membrane proteins: Detection of spectrin oligomers by gel electrophoresis
Morrow J, Haigh W. [23] Erythrocyte membrane proteins: Detection of spectrin oligomers by gel electrophoresis. Methods In Enzymology 1983, 96: 298-304. PMID: 6656632, DOI: 10.1016/s0076-6879(83)96027-5.Peer-Reviewed Original ResearchMeSH KeywordsElectrophoresis, Polyacrylamide GelErythrocyte MembraneHumansIndicators and ReagentsMacromolecular SubstancesMolecular WeightRosaniline DyesSpectrinConceptsSodium dodecyl sulfateDodecyl sulfateGel electrophoresisPolyacrylamide gel electrophoresisGelMembrane proteinsProtein-protein associationSlab gelsOligomersSecond dimensionSpectrin oligomersElectrophoretic analysisPrincipal structural proteinPreparationErythrocyte membrane skeletonPolyacrylamide gel electrophoretic analysisErythrocyte membrane proteinsElectrophoresisGel electrophoretic analysisNondenaturing gelMembrane skeletonDistinct polypeptidesStructural proteinsSpectrin moleculesMolecules
1982
A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains.
Speicher D, Morrow J, Knowles W, Marchesi V. A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains. Journal Of Biological Chemistry 1982, 257: 9093-9101. PMID: 7096353, DOI: 10.1016/s0021-9258(18)34247-9.Peer-Reviewed Original ResearchMeSH KeywordsElectrophoresis, Cellulose AcetateElectrophoresis, Polyacrylamide GelErythrocytesHumansMacromolecular SubstancesMembrane ProteinsModels, ChemicalMolecular WeightPeptide FragmentsSpectrinTrypsinConceptsNumerous small peptidesPeptide mapping techniquesChemical domainsPeptide segmentsMolecular weightChemical cleavageSized peptidesTwo-dimensional peptide mapping techniquesSmall peptidesIntact moleculeUnique peptidesPhosphorylated amino acidsFurther proteolytic cleavageOverlap peptidesPolypeptide segmentsIntermediate-sized peptidesMoleculesMild trypsin digestionTrypsin digestionTwo-dimensional peptide mapsPeptidesStructural modelSpectrin subunitsCleavagePeptide maps