2003
Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis
Williams S, Smith A, Cianci C, Morrow J, Brown T. Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis. Apoptosis 2003, 8: 353-361. PMID: 12815278, DOI: 10.1023/a:1024168901003.Peer-Reviewed Original ResearchConceptsCaspase-3 cleavage siteCleavage sitePrimary cleavage siteII-spectrinCytoskeletal integrityAlpha II spectrinMembrane stabilityCaspase-3Cleavage of alphaApoptotic cell deathCaspase-3 activationMature B cellsConsensus sitesDeletion analysisTranscriptional inhibitorMajor proteinsLikely altersApoptotic bodiesCell deathProteinStructural conformationActinomycin DSpectrinNew insightsApoptosis
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
Calpain proteolysis of αII-spectrin in the normal adult human brain
Huh G, Glantz S, Je S, Morrow J, Kim J. Calpain proteolysis of αII-spectrin in the normal adult human brain. Neuroscience Letters 2001, 316: 41-44. PMID: 11720774, DOI: 10.1016/s0304-3940(01)02371-0.Peer-Reviewed Original ResearchConceptsAdult human brainCalpain activationEvident neurological diseaseHuman brainCortical gray matterLong-term potentiationNormal adult human brainDendrites of neuronsCerebellar Purkinje cellsCalpain processingReactive astrocytesCerebral cortexPyramidal neuronsSynaptic remodelingClinical conditionsNeuronal apoptosisAdult brainPositive cellsNeurological diseasesGray matterPurkinje cellsTopographic distributionAlphaII-spectrinBrainCalpain proteolysisDynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
Zhang Z, Weed S, Gallagher P, Morrow J. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain. Blood 2001, 98: 1645-1653. PMID: 11535493, DOI: 10.1182/blood.v98.6.1645.Peer-Reviewed Original ResearchConceptsSelf-association domainPoint mutationsHuman sequenceDrosophila alpha-spectrinDynamic molecular modelingHuman erythrocyte spectrinCytoskeletal functionSpecific point mutationsConservative substitutionsPrimary sequenceConformational rearrangementsAlpha-spectrinHelical regionHydrophilic residuesAmino acidsMutationsSpectrinSalt bridgeErythrocyte spectrinStructural consequencesPathogenic mutationsRepeat unitsMolecular modelingSequenceStructural disruptionβIII 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 spectrinSpectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias?
Giorgi M, Cianci C, Gallagher P, Morrow J. Spectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias? Experimental And Molecular Pathology 2001, 70: 215-230. PMID: 11418000, DOI: 10.1006/exmp.2001.2377.Peer-Reviewed Original Research[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 strategiesPeptidesMembraneCellsOrganellesCaspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*
Lee A, Morrow J, Fowler V. Caspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*. Journal Of Biological Chemistry 2001, 276: 20735-20742. PMID: 11278555, DOI: 10.1074/jbc.m009723200.Peer-Reviewed Original ResearchConceptsLens fiber cellsFiber cellsMembrane blebbingMembrane skeletonLens developmentAlpha-spectrinSpectrin membrane skeletonMembrane skeleton componentsChick lens developmentCell-cell fusionApoptotic cellsOldest fiber cellsMembrane associationClassical apoptosisApoptotic processSpecific proteolysisTerminal differentiationAdult lensSpectrin fragmentsMembrane interdigitationsBlebbingCytoskeletal protein alpha-spectrinPermanent remodelingSkeleton componentsSpectrinDynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids
Muresan V, Stankewich M, Steffen W, Morrow J, Holzbaur E, Schnapp B. Dynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids. Molecular Cell 2001, 7: 173-183. PMID: 11172722, DOI: 10.1016/s1097-2765(01)00165-4.Peer-Reviewed Original ResearchConceptsVesicle transportAcidic phospholipidsAxonal vesiclesProtein-free liposomesAbsence of membranesPH domainDependent motilityCytosolic factorsDynactinSpectrinEssential roleSpectrin polypeptidesVesiclesMembranePhospholipidsAxonal transportMotilitySoluble componentsContext of liposomesDyneinCytosolPolypeptideTransportRoleRetrograde axonal transport
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 ResearchConceptsInteraction 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 βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210
Stabach P, Morrow J. Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210. Journal Of Biological Chemistry 2000, 275: 21385-21395. PMID: 10764729, DOI: 10.1074/jbc.c000159200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCloning, MolecularConsensus SequenceDNA, ComplementaryDrosophilaDrosophila ProteinsExonsGene LibraryHumansIntronsMammalsMolecular Sequence DataMolecular WeightOrgan SpecificityPhylogenyRatsRecombinant ProteinsRepetitive Sequences, Amino AcidRetinaSequence AlignmentSequence Homology, Amino AcidSpectrinTumor Cells, CulturedViral ProteinsConceptsDrosophila orthologMammalian orthologsSpectrin repeatsPleckstrin homology domainComplete cDNA sequenceActin-binding domainSelf-association domainAmino acids 85Amino acid sequenceBeta-spectrin geneHuman retina cDNA libraryRetina cDNA libraryFly counterpartMammalian spectrinsCaenorhabditis elegansHomology domainEpithelial cell populationsSH3 domainApical domainCDNA sequenceCDNA libraryOrthologsPolarized epitheliumBeta spectrinAcid sequenceSpectrin tethers and mesh in the biosynthetic pathway.
De Matteis M, Morrow J. Spectrin tethers and mesh in the biosynthetic pathway. Journal Of Cell Science 2000, 113 ( Pt 13): 2331-43. PMID: 10852813, DOI: 10.1242/jcs.113.13.2331.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCytoskeletonGolgi ApparatusHumansIntracellular MembranesProtein BiosynthesisSpectrinConceptsSecretory pathwayMembrane proteinsSmall GTPase ArfEarly secretory pathwayDynamics of organellesGolgi dynamicsProtein traffickingOrganelle functionGolgi structurePhosphoinositide levelsGolgi membranesBiosynthetic pathwayMacromolecular complexesCytosolic proteinsAdapter moleculeSpectrin skeletonIntracellular transportOrganellesSpectrinDirect interactionProteinKey playersRecent discoveryGolgiSimilar role
1999
Brain and Muscle Express a Unique Alternative Transcript of αΙΙ Spectrin †
Cianci C, Zhang Z, Pradhan D, Morrow J. Brain and Muscle Express a Unique Alternative Transcript of αΙΙ Spectrin †. Biochemistry 1999, 38: 15721-15730. PMID: 10625438, DOI: 10.1021/bi991458k.Peer-Reviewed Original ResearchConceptsAlternative mRNA splicingMRNA splicingAlphaII-spectrinBp insertionNovel protein interaction siteEmbryonic tissuesInsert 2Alternative exon usageProtein interaction sitesAmino acid sequenceDifferent splice formsAmino acid insertionMouse embryonic tissuesInsert-1Amino acid substitutionsSkeletal muscleGene familyDynamic molecular modelingMature proteinUnanticipated functionAlternative splicingExon usageIndividual transcriptsAlternative transcriptsSplice forms
1998
A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles
Stankewich M, Tse W, Peters L, Ch’ng Y, John K, Stabach P, Devarajan P, Morrow J, Lux S. A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14158-14163. PMID: 9826670, PMCID: PMC24343, DOI: 10.1073/pnas.95.24.14158.Peer-Reviewed Original ResearchConceptsBetaIII spectrinGene mapsMembrane skeletonEndoplasmic reticulum marker calnexinPlasma membrane skeletonPleckstrin homology domainTrans-Golgi networkHuman brain cDNASyntenic regionsGene familyProtein 4.1Membrane associationCompartment markersImportant structural componentDa proteinSelf-association siteGolgi membranesHomology searchCDNA endsRapid amplificationUnidentified isoformChromosome 19Liver Golgi membranesGenBank databaseVesicle markersThe role of ankyrin and spectrin in membrane transport and domain formation
De Matteis M, Morrow J. The role of ankyrin and spectrin in membrane transport and domain formation. Current Opinion In Cell Biology 1998, 10: 542-549. PMID: 9719877, DOI: 10.1016/s0955-0674(98)80071-9.Peer-Reviewed Original ResearchConceptsAnterograde protein traffickingRole of ankyrinADP-ribosylation factorGolgi integrityProtein traffickingSpecific functional domainsSpectrin functionSecretory pathwayMotor proteinsFunctional domainsGolgi complexMembrane transportNovel insightsSpectrinRecent discoveryDomain formationAnkyrinTraffickingProteinPathwayFunctionComplexesDiscoveryDomainIdentificationSimultaneous Degradation of αII- and βII-Spectrin by Caspase 3 (CPP32) in Apoptotic Cells*
Wang K, Posmantur R, Nath R, McGinnis K, Whitton M, Talanian R, Glantz S, Morrow J. Simultaneous Degradation of αII- and βII-Spectrin by Caspase 3 (CPP32) in Apoptotic Cells*. Journal Of Biological Chemistry 1998, 273: 22490-22497. PMID: 9712874, DOI: 10.1074/jbc.273.35.22490.Peer-Reviewed Original ResearchADP 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
1997
Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells
Devarajan P, Stabach P, De Matteis M, Morrow J. Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 10711-10716. PMID: 9380700, PMCID: PMC23456, DOI: 10.1073/pnas.94.20.10711.Peer-Reviewed Original ResearchConceptsMembrane proteinsEndoplasmic reticulumSpectrin skeletonVesicular tubular clustersActin-binding domainSpecific membrane proteinsMadin-Darby canine kidney cellsK-ATPase transportCanine kidney cellsDynactin complexVesicle traffickingCargo proteinsGolgi spectrinTrafficking systemBeta-COPMembrane compartmentsTransport of alphaAdapter proteinCis-GolgiGolgi membranesGolgi stacksDocking complexBetaI spectrinGolgiBeta NASite-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
1996
Entorhinal cortical innervation of parvalbumin‐containing neurons (basket and chandelier cells) in the rat ammon's horn
Kiss J, Buzsaki G, Morrow J, Glantz S, Leranth C. Entorhinal cortical innervation of parvalbumin‐containing neurons (basket and chandelier cells) in the rat ammon's horn. Hippocampus 1996, 6: 239-246. PMID: 8841824, DOI: 10.1002/(sici)1098-1063(1996)6:3<239::aid-hipo3>3.0.co;2-i.Peer-Reviewed Original ResearchConceptsEntorhinal cortex lesionPyramidal cellsHippocampal sectionsCortex lesionsEntorhinal cortical axonsParvalbumin-containing neuronsShort-latency inhibitionAsymmetric synaptic contactsActivity of interneuronsInhibitory basketPerisomatic areaChandelier cellsCortical efferentsDendritic shaftsHippocampal areaSynaptic contactsAmmon's hornCortical innervationAnterograde tracerCA3 regionCortical axonsEntorhinal inputElectron microscopic studyFeed-forward activationInterneurons