2001
βIII Spectrin Binds to the Arp1 Subunit of Dynactin*
Holleran E, Ligon L, Tokito M, Stankewich M, Morrow J, Holzbaur E. βIII Spectrin Binds to the Arp1 Subunit of Dynactin*. Journal Of Biological Chemistry 2001, 276: 36598-36605. PMID: 11461920, DOI: 10.1074/jbc.m104838200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBrainCell MembraneCOS CellsCytoplasmCytosolDynactin ComplexElectrophoresis, Polyacrylamide GelGlutathione TransferaseImmunoblottingImmunohistochemistryMicrofilament ProteinsMicrotubule-Associated ProteinsPrecipitin TestsProtein BindingProtein IsoformsProtein Structure, TertiaryRatsSpectrinSrc Homology DomainsTwo-Hybrid System TechniquesConceptsBetaIII spectrinGolgi vesicle traffickingMicrotubule motor complexAssociation of dyneinVesicle traffickingVesicular cargoRat brain cytosolMitotic spindleIntracellular motorsCytoplasmic dyneinCleavage furrowDynactinInterphase cellsArp1Spectrin isoformsCytoplasmic vesiclesF-actinActin bindsEndoplasmic reticulumPerinuclear regionNovel localizationSpectrinDyneinBrain cytosolΒIII spectrinDynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids
Muresan V, Stankewich M, Steffen W, Morrow J, Holzbaur E, Schnapp B. Dynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids. Molecular Cell 2001, 7: 173-183. PMID: 11172722, DOI: 10.1016/s1097-2765(01)00165-4.Peer-Reviewed Original ResearchConceptsVesicle transportAcidic phospholipidsAxonal vesiclesProtein-free liposomesAbsence of membranesPH domainDependent motilityCytosolic factorsDynactinSpectrinEssential roleSpectrin polypeptidesVesiclesMembranePhospholipidsAxonal transportMotilitySoluble componentsContext of liposomesDyneinCytosolPolypeptideTransportRoleRetrograde axonal transport
1993
The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons.
Malchiodi-Albedi F, Ceccarini M, Winkelmann J, Morrow J, Petrucci T. The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons. Journal Of Cell Science 1993, 106 ( Pt 1): 67-78. PMID: 8270644, DOI: 10.1242/jcs.106.1.67.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAstrocytesCerebellar CortexErythrocytesMicrotubule-Associated ProteinsMolecular Sequence DataNeuronsPurkinje CellsRNA SplicingSpectrinSynapsesSynapsinsConceptsBeta IPostsynaptic densityMultiple alternative transcriptsBeta-spectrin isoformBeta-spectrin genePlasma membrane stainingAlpha beta heterodimersNon-erythroid alpha-spectrinRegion of alphaCerebellar granule cellsDistinct genesPrecise segregationSubstantial homologyBiochemical restrictionsSingle protein bandAlternative transcriptsDistinct cytoplasmicUnique sequencesCerebellar neuronsSpectrin isoformsBeta heterodimerAlpha-spectrinSpectrin complexSplice variantsTargeting mechanism
1987
Synapsin I: an actin-bundling protein under phosphorylation control.
Petrucci T, Morrow J. Synapsin I: an actin-bundling protein under phosphorylation control. Journal Of Cell Biology 1987, 105: 1355-1363. PMID: 3115996, PMCID: PMC2114810, DOI: 10.1083/jcb.105.3.1355.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBrainCattleKineticsMicrotubule-Associated ProteinsMicrotubulesNerve Tissue ProteinsPhosphoproteinsPhosphorylationSynapsinsConceptsMicrotubule-binding activity