2006
Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat
Stankewich MC, Stabach PR, Morrow JS. Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat. Journal Of Cell Science 2006, 119: 958-969. PMID: 16495487, DOI: 10.1242/jcs.02751.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCarrier ProteinsCell LineCells, CulturedChlorocebus aethiopsCloning, MolecularCOP-Coated VesiclesCOS CellsExonsGene Expression RegulationHumansMolecular Sequence DataPhosphoproteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentVesicular Transport ProteinsConceptsCOPII coatProline-rich C-terminal regionEndoplasmic reticulumTerminal proline-rich regionCOPII vesicle coatVesicular tubular clustersProline-rich regionWD repeat domainFull-length proteinAlternative mRNA splicingN-terminal domainC-terminal regionVesicle coatWD repeatsMammalian orthologuesVesicular trafficSecretory pathwayMRNA splicingExon utilizationExon 13Sec31pChromosome 10q24Gene productsSec31BSpecialized functions
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
1998
Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1
Sinard J, Stewart G, Stabach P, Argent A, Gilligan D, Morrow J. Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1. Biochimica Et Biophysica Acta 1998, 1396: 57-66. PMID: 9524222, DOI: 10.1016/s0167-4781(97)00167-x.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceBase SequenceCalmodulin-Binding ProteinsCloning, MolecularExonsHumansIntracellular Signaling Peptides and ProteinsIsomerismMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstrateOrgan SpecificityPolymerase Chain ReactionProtein Structure, TertiaryProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsNovel amino acidAmino acidsBeta-adducinNew isoformHuman bone marrow cDNA libraryBone marrow cDNA libraryDifferent reading framesCalcium/calmodulinLysine-rich sequenceNT-2 cellsProtein kinase CGenomic clonesGenomic mapNew amino acidsAlternate exonsActin crossCDNA libraryReading frameSplice consensus sequenceNew exonsNovel isoformConsensus sequenceStop codonKinase CExons
1997
Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin