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 interactions
1998
Structure 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
1996
Chapter 6 The Spectrin Cytoskeleton and Organization of Polarized Epithelial Cell Membranes
Devarajan P, Morrow J. Chapter 6 The Spectrin Cytoskeleton and Organization of Polarized Epithelial Cell Membranes. Current Topics In Membranes 1996, 43: 97-128. DOI: 10.1016/s0070-2161(08)60386-x.Peer-Reviewed Original ResearchIntegral membrane proteinsPeripheral plasma membraneCultured epithelial cellsEpithelial cellsAnti-spectrin antibodiesEukaryotic cellsNonerythroid cellsMembrane proteinsSpectrin cytoskeletonEpithelial cell membranesPlasma membraneExperimental removalCell shapeDifferent isoformsMembrane stabilitySpectrinCell membraneCytoskeletonPostsynaptic densityPostsynaptic membraneMembrane instabilityCerebellar granule cellsSkeletal muscleMembraneCells
1994
Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2).
Lombardo C, Weed S, Kennedy S, Forget B, Morrow J. Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2). Journal Of Biological Chemistry 1994, 269: 29212-29219. PMID: 7961888, DOI: 10.1016/s0021-9258(19)62032-6.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainBeta II spectrinHomology domainSequence motifsBeta III-spectrinBrain spectrinGlutathione S-transferase fusion proteinRepeat 1S-transferase fusion proteinMembrane association domainNovel functional motifsCOOH-terminal domainG protein bindingDistinct sequence motifsBovine brain spectrinCOOH-terminal sequenceAssociation domainMembrane associationProtein 4.1Spectrin functionSequence comparisonPlasma membraneFunctional motifsRecombinant proteins
1991
Chapter 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
Fodrin as a differentiation marker. Redistributions in colonic neoplasia.
Younes M, Harris A, Morrow J. Fodrin as a differentiation marker. Redistributions in colonic neoplasia. American Journal Of Pathology 1989, 135: 1197-212. PMID: 2596576, PMCID: PMC1880505.Peer-Reviewed Original ResearchConceptsPolarized epithelial cellsDistribution of fodrinImmunofluorescent confocal microscopyMadin-Darby canine kidney cellsCultured Madin-Darby canine kidney (MDCK) cellsMicrovillar brush borderCanine kidney cellsCell polarityCytoplasmic faceDisease samplesPlasma membraneReceptor domainPathologic stressMature cellsMDCK cellsFodrinDifferentiation markersTerminal webConfocal microscopyVillus maturationKidney cellsPrecise roleEpithelial cellsCrohn's disease samplesTotal pool
1987
Spectrin Is Associated With Membrane-Bound Actin Filaments in Platelets and Is Hydrolyzed by the Ca2+-Dependent Protease During Platelet Activation
Fox J, Reynolds C, Morrow J, Phillips D. Spectrin Is Associated With Membrane-Bound Actin Filaments in Platelets and Is Hydrolyzed by the Ca2+-Dependent Protease During Platelet Activation. Blood 1987, 69: 537-545. DOI: 10.1182/blood.v69.2.537.537.Peer-Reviewed Original ResearchActin filamentsDependent proteasePlasma membraneRBC spectrinSubmembranous actin filamentsActin-binding proteinsBeta chainMembrane-bound filamentsActin filament networkTriton XImmunoprecipitation experimentsMinor polypeptidesFilament networkSpectrinGlycoprotein IbBrain spectrinDifferential centrifugationPresence of Ca2ProteaseLysatesPolyacrylamide gelsUnstimulated plateletsPolypeptideUnidentified componentsN-ethylmaleimide