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
1998
The 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 formationAnkyrinTraffickingProteinPathwayFunctionComplexesDiscoveryDomainIdentificationStructure 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
Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton
Morrow J, Rimm D, Kennedy S, Cianci C, Sinard J, Weed S. Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton. 1997, 485-540. DOI: 10.1002/cphy.cp140111.Peer-Reviewed Original ResearchNon-erythroid cellsMembrane skeletonRed cell membrane skeletonSpectrin membrane skeletonCell membrane skeletonErythrocyte membrane skeletonMembrane organizersProtein 4.1Spectrin cytoskeletonAdhesion proteinsCytoskeletal elementsSpectrin skeletonMembrane stabilityMosaic modelSpectrinProteinCellsDematinDynaminStomatinPallidinCytoskeletonAnkyrinAdducinTropomodulin
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
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 unitsCDNAChapter 14 Polarized Assembly of Spectrin and Ankyrin in Epithelial Cells
Morrow J, Cianci C, Kennedy S, Warren S. Chapter 14 Polarized Assembly of Spectrin and Ankyrin in Epithelial Cells. Current Topics In Membranes 1991, 38: 227-244. DOI: 10.1016/s0070-2161(08)60791-1.Peer-Reviewed Original ResearchSpectrin skeletonAmino terminusRed cell skeletonPost-translational controlBind F-actinSpectrin-actin cytoskeletonInteraction of spectrinRole of proteinsProtein 4.9Protein 4.1Signal transductionSpectrin cytoskeletonAccessory proteinsPlasma membranePolarized assemblySubunit interactionsF-actinΒ-subunitAnkyrinCell skeletonMembrane transportSpectrin-ankyrin interactionSpectrinAntiparallel heterodimerCytoskeleton
1989
Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.
Morrow J, Cianci C, Ardito T, Mann A, Kashgarian M. Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. Journal Of Cell Biology 1989, 108: 455-465. PMID: 2537316, PMCID: PMC2115445, DOI: 10.1083/jcb.108.2.455.Peer-Reviewed Original ResearchConceptsMadin-Darby canine kidney cellsCanine kidney cellsK-ATPaseAlpha subunitMolecular mechanismsMDCK cellsMinor membrane proteinsDistribution of fodrinErythrocyte ankyrinConfluent MDCK cellsBinding of ankyrinKidney cellsHuman erythrocyte ankyrinRenal epithelial cellsCytoplasmic domainNonerythroid cellsMembrane proteinsCortical cytoskeletonBasolateral domainMembrane skeletonPolarized distributionAnkyrinBasolateral marginsCell developmentErythrocyte band 3
1988
Phosphorylation of ankyrin down‐regulates its cooperative interaction with spectrin and protein 3
Cianci C, Giorgi M, Morrow J. Phosphorylation of ankyrin down‐regulates its cooperative interaction with spectrin and protein 3. Journal Of Cellular Biochemistry 1988, 37: 301-315. PMID: 2970468, DOI: 10.1002/jcb.240370305.Peer-Reviewed Original ResearchConceptsCytoplasmic domainAffinity of ankyrinProtein 3Integral membrane proteinsSpectrin tetramersCooperative interactionsSpectrin oligomersMembrane kinaseSpectrin dimersLong-range cooperative interactionsNonerythroid cellsProtein phosphorylationMembrane proteinsPeripheral cytoskeletonBeta spectrinAnkyrinPhosphorylationOligomer formationChymotryptic digestionSpectrinPrimary attachmentGeneral importanceCooperative fashionEnhanced affinitySuch interactions