2000
Spectrin 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 roleIdentification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*
Wang Y, Morrow J. Identification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*. Journal Of Biological Chemistry 2000, 275: 8062-8071. PMID: 10713127, DOI: 10.1074/jbc.275.11.8062.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntibody SpecificityBlood ProteinsCloning, MolecularCytoskeletonDNA, ComplementaryErythrocyte MembraneHumansMembrane ProteinsMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsProtein BindingProtein BiosynthesisProtein Structure, TertiarySequence Analysis, DNASequence Analysis, ProteinSequence Homology, Amino AcidTissue DistributionConceptsIntegral membrane proteinsMembrane proteinsStomatin homologueSLP-1SLP-2Human stomatinCholesterol-rich lipid raftsLipid domain organizationTerminal hydrophobic domainAmino acid sequenceCultured COS cellsMature human erythrocytesSDS-polyacrylamide gel electrophoresis analysisErythrocyte membrane proteinsDomain organizationNonerythroid tissuesLipid raftsStomatin genePeripheral cytoskeletonChromosome 9p13StomatinAcid sequenceGel electrophoresis analysisCOS cellsRelated proteins
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
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
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
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
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 ResearchConceptsSodium 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