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 spectrin
1991
Actin and tubulin binding domains of synapsins Ia and Ib.
Petrucci T, Morrow J. Actin and tubulin binding domains of synapsins Ia and Ib. Biochemistry 1991, 30: 413-22. PMID: 1899024, DOI: 10.1021/bi00216a016.Peer-Reviewed Original Research
1990
Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions
BECKER P, SCHWARTZ M, MORROW J, Samuel E. Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions. The FEBS Journal 1990, 193: 827-836. PMID: 2249696, DOI: 10.1111/j.1432-1033.1990.tb19406.x.Peer-Reviewed Original ResearchCalmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin.
Harris A, Morrow J. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 3009-3013. PMID: 2326262, PMCID: PMC53823, DOI: 10.1073/pnas.87.8.3009.Peer-Reviewed Original Research
1989
An unusual beta-spectrin associated with clustered acetylcholine receptors.
Bloch R, Morrow J. An unusual beta-spectrin associated with clustered acetylcholine receptors. Journal Of Cell Biology 1989, 108: 481-493. PMID: 2645300, PMCID: PMC2115447, DOI: 10.1083/jcb.108.2.481.Peer-Reviewed Original ResearchContributions of the β‐subunit to spectrin structure and function
Coleman T, Fishkind D, Mooseker M, Morrow J. Contributions of the β‐subunit to spectrin structure and function. Cytoskeleton 1989, 12: 248-263. PMID: 2524283, DOI: 10.1002/cm.970120406.Peer-Reviewed Original Research
1988
A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Petrucci T, Mooseker M, Morrow J. A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin. Journal Of Cellular Biochemistry 1988, 36: 25-35. PMID: 3125185, DOI: 10.1002/jcb.240360104.Peer-Reviewed Original ResearchConceptsBovine synapsin ISynapsin IActin binding proteinsPeptide mappingTwo-dimensional peptide mapsSmall synaptic vesiclesPhosphorylation controlBundling proteinActin bindingUnrelated proteinsActin bundlesActin filamentsNeuronal phosphoproteinSynapsin I.Binding proteinVivo roleSynaptic vesiclesParent proteinProteinPeptide mapsChymotryptic digestionVillinPeptide fragmentsCross reactFragments
1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Mische S, Mooseker M, Morrow J. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. Journal Of Cell Biology 1987, 105: 2837-2845. PMID: 3693401, PMCID: PMC2114693, DOI: 10.1083/jcb.105.6.2837.Peer-Reviewed Original ResearchSynapsin 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 ResearchBeta 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
1982
The Polymeric State of Actin in the Human Erythrocyte Cytoskeleton
Atkinson M, Morrow J, Marchesi V. The Polymeric State of Actin in the Human Erythrocyte Cytoskeleton. Journal Of Cellular Biochemistry 1982, 18: 493-505. PMID: 7200988, DOI: 10.1002/jcb.1982.240180410.Peer-Reviewed Original Research