2000
Identification 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 sequence
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 unitsCDNA
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
1987
Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
Coleman T, Harris A, Mische S, Mooseker M, Morrow J. Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions. Journal Of Cell Biology 1987, 104: 519-526. PMID: 3818791, PMCID: PMC2114562, DOI: 10.1083/jcb.104.3.519.Peer-Reviewed Original Research
1986
Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin
Harris A, Anderson J, Yurchenco P, Green L, Ainger K, Morrow J. Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin. Journal Of Cellular Biochemistry 1986, 30: 51-69. PMID: 2420811, DOI: 10.1002/jcb.240300107.Peer-Reviewed Original Research