2000
βiv Spectrin, a New Spectrin Localized at Axon Initial Segments and Nodes of Ranvier in the Central and Peripheral Nervous System
Berghs S, Aggujaro D, Dirkx R, Maksimova E, Stabach P, Hermel J, Zhang J, Philbrick W, Slepnev V, Ort T, Solimena M. βiv Spectrin, a New Spectrin Localized at Axon Initial Segments and Nodes of Ranvier in the Central and Peripheral Nervous System. Journal Of Cell Biology 2000, 151: 985-1002. PMID: 11086001, PMCID: PMC2174349, DOI: 10.1083/jcb.151.5.985.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnkyrinsAutoantigensAxonsBlood ProteinsBrain ChemistryChromosomesCloning, MolecularCOS CellsCytoplasmCytoskeletonDiabetic NeuropathiesGene ExpressionHippocampusHumansIslets of LangerhansMaleMembrane ProteinsMiceMolecular Sequence DataNerve Tissue ProteinsPhosphoproteinsProtein Structure, TertiaryProtein Tyrosine PhosphatasesRanvier's NodesRatsRats, Sprague-DawleyReceptor-Like Protein Tyrosine Phosphatases, Class 8RNA, MessengerSciatic NerveSignal TransductionSodium ChannelsSpectrinConceptsPleckstrin homology domainHomology domainBetaIV spectrinActin-binding domainAxon initial segmentPutative SH3Alternative splicingSpectrin geneSpectrin repeatsDetergent extractabilityCell adhesion moleculeNodes of RanvierSubcellular fractionationTerminal halfAdditional isoformsDistinct isoformsLong isoformNorthern blotSpectrinAbundant expressionΒIV-spectrinIsoformsSpectrin antibodiesEmbryonic day 19Initial segmentIdentification 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
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