2010
Ankyrin recognizes both surface character and shape of the 14–15 di-repeat of β-spectrin
La-Borde PJ, Stabach PR, Simonović I, Morrow JS, Simonović M. Ankyrin recognizes both surface character and shape of the 14–15 di-repeat of β-spectrin. Biochemical And Biophysical Research Communications 2010, 392: 490-494. PMID: 20079712, PMCID: PMC2839365, DOI: 10.1016/j.bbrc.2010.01.046.Peer-Reviewed Original ResearchConceptsMinimal recognition motifRecognition motifMembrane protein traffickingSpectrin-based cytoskeletonDistinct recognition mechanismsSite-directed mutagenesisComplementary surface chargesHigh-affinity complexProtein traffickingMembrane organizationBeta spectrinLinker mutationsΒ-spectrinBinding surfaceIsothermal titration calorimetryAnkyrinRecognition mechanismTitration calorimetry
2008
Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells
Stabach PR, Devarajan P, Stankewich MC, Bannykh S, Morrow JS. Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells. American Journal Of Physiology - Cell Physiology 2008, 295: c1202-c1214. PMID: 18768923, PMCID: PMC2584975, DOI: 10.1152/ajpcell.00273.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnkyrin RepeatAnkyrinsCell PolarityChlorocebus aethiopsCOS CellsCytoplasmDogsEndoplasmic ReticulumGolgi ApparatusHumansMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein ConformationProtein FoldingProtein Sorting SignalsProtein TransportRatsRecombinant Fusion ProteinsRNA InterferenceRNA, Small InterferingSodium-Potassium-Exchanging ATPaseTime FactorsTransfectionViral Envelope ProteinsConceptsEndoplasmic reticulumSecretory pathwayPlasma membraneVesicular stomatitis virus G proteinMadin-Darby canine kidney cellsVirus G proteinSmall hairpin RNACanine kidney cellsGolgi traffickingAnkyrin RGolgi transportSemipermeabilized cellsER retentionCytoplasmic domainMembrane proteinsAssembly pathwayProtein ankyrinIntracellular traffickingAnkyrinFusion proteinSimilar phenotypeG proteinsSuch phenotypesHairpin RNACultured cells
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
1996
The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle.
Weed SA, Stabach PR, Oyer CE, Gallagher PG, Morrow JS. The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle. Laboratory Investigation 1996, 74: 1117-29. PMID: 8667615.Peer-Reviewed Original ResearchConceptsBeta ISpectrin skeletonSkeletal muscleMost such mutationsGene transferAdult mouse skeletal muscleDominant-negative fashionErythroid lineage cellsNeonatal skeletal muscleCultured muscle cellsAlpha beta heterodimersErythrocyte shape abnormalitiesMuscle cellsMouse skeletal muscleDefective proteinSpectrin geneAlternative transcriptsHemolytic phenotypeCDNA constructsNull phenotypeC2C12 myoblastsBeta heterodimerSpectrin mutationsSedimentation velocity analysisIntracellular distribution