2022
CECR2 drives breast cancer metastasis by promoting NF-κB signaling and macrophage-mediated immune suppression
Zhang M, Liu ZZ, Aoshima K, Cai WL, Sun H, Xu T, Zhang Y, An Y, Chen JF, Chan LH, Aoshima A, Lang SM, Tang Z, Che X, Li Y, Rutter SJ, Bossuyt V, Chen X, Morrow JS, Pusztai L, Rimm DL, Yin M, Yan Q. CECR2 drives breast cancer metastasis by promoting NF-κB signaling and macrophage-mediated immune suppression. Science Translational Medicine 2022, 14: eabf5473. PMID: 35108062, PMCID: PMC9003667, DOI: 10.1126/scitranslmed.abf5473.Peer-Reviewed Original ResearchConceptsBreast cancer metastasisReticuloendotheliosis viral oncogene homolog ACancer metastasisImmune suppressionM2 macrophagesWorse metastasis-free survivalMetastatic breast cancerMetastasis-free survivalV-rel avian reticuloendotheliosis viral oncogene homolog ACancer-related deathPrimary breast tumorsMultiple mouse modelsNF-κB signalingImmunocompetent settingNuclear factor-κB family membersMetastasis-promoting genesDistant metastasisMetastatic sitesPrimary tumorEffective therapyBreast cancerMetastasis treatmentMouse modelBreast tumorsMetastasis
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
2001
Dynamic 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 spectrinDynactin-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 transportCaspase 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 componentsSpectrin[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 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 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-spectrinIdentification 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 ResearchConceptsSecretory 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 formsTransforming Growth Factor β Induces Caspase 3-independent Cleavage of αII-Spectrin (α-Fodrin) Coincident with Apoptosis*
Brown T, Patil S, Cianci C, Morrow J, Howe P. Transforming Growth Factor β Induces Caspase 3-independent Cleavage of αII-Spectrin (α-Fodrin) Coincident with Apoptosis*. Journal Of Biological Chemistry 1999, 274: 23256-23262. PMID: 10438500, DOI: 10.1074/jbc.274.33.23256.Peer-Reviewed Original ResearchConceptsAlphaII-spectrinBroad-spectrum caspase inhibitorDistinct apoptotic pathwaysImmature B cell linesOnset of apoptosisCaspase-3 activationInduction of apoptosisPotent growth inhibitorNovel caspaseCaspase inhibitorsWEHI-231Cytoskeletal actinApoptotic pathwayB cell linesNovel substrateCell deathGrowth factor betaFirst direct evidenceCaspase-3ApoptosisCell linesCaspasesGrowth inhibitorFactor betaFirst evidence
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 markersADP 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 fractionsProteinPtdInsP2Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*
Zhang Z, Devarajan P, Dorfman A, Morrow J. Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*. Journal Of Biological Chemistry 1998, 273: 18681-18684. PMID: 9668035, DOI: 10.1074/jbc.273.30.18681.Peer-Reviewed Original ResearchConceptsK-ATPaseUbiquitous membrane proteinsSecond cytoplasmic domainSpecific macromolecular interactionsMadin-Darby canine kidney cellsAlpha-NACanine kidney cellsCytoplasmic domainThree-dimensional structureMembrane proteinsGlutathione S-transferasePlasma membraneRegulatory proteinsAnkyrinAmino acids bindFusion proteinResidues 142Trisphosphate receptorVectorial transportSurface loopsMacromolecular interactionsMultiple ankyrinHydrophilic faceS-transferaseFusion peptide
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 NA
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
1994
Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the αEβ7 integrin
Cepek K, Shaw S, Parker C, Russell G, Morrow J, Rimm D, Brenner M. Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the αEβ7 integrin. Nature 1994, 372: 190-193. PMID: 7969453, DOI: 10.1038/372190a0.Peer-Reviewed Original ResearchConceptsIntraepithelial lymphocytesAdhesion moleculesT cellsIntestinal intra-epithelial lymphocytesEpithelial cellsIntestinal intraepithelial lymphocytesIntra-epithelial lymphocytesMucosal immune systemE-cadherinTissue-specific retentionTissue-specific compartmentalizationLymphoid structuresT lymphocytesImmune systemLymphocyte homingLymphocytesΑEβ7
1993
Cloning of a Portion of the Chromosomal Gene and cDNA for Human β-Fodrin, the Nonerythroid Form of β-Spectrin
Chang J, Scarpa A, Eddy R, Byers M, Harris A, Morrow J, Watkins P, Shows T, Forget B. Cloning of a Portion of the Chromosomal Gene and cDNA for Human β-Fodrin, the Nonerythroid Form of β-Spectrin. Genomics 1993, 17: 287-293. PMID: 8406479, DOI: 10.1006/geno.1993.1323.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCarrier ProteinsChromosome MappingChromosomes, Human, Pair 2Cloning, MolecularDNA ProbesDNA, ComplementaryExonsHumansHybrid CellsIntronsMiceMicrofilament ProteinsMolecular Sequence DataNerve Tissue ProteinsOligonucleotide ProbesRestriction MappingSequence Homology, Amino AcidSpectrinConceptsAmino acid sequenceAcid sequenceNonerythroid formsDNA sequencesSimilar exon/intron organizationGenomic DNAExon/intron organizationSomatic hybrid cell linesCell cDNA libraryHuman genomic librarySingle-copy DNA fragmentsSingle-copy probesComposite DNA sequenceDNA sequence analysisHybrid cell linesIntron organizationChromosomal localizationGenomic clonesGenomic libraryGenomic fragmentChromosomal genesCDNA clonesCDNA libraryChromosome 2Nucleotide sequence