2001
[42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex
De Matteis M, Morrow J. [42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex. Methods In Enzymology 2001, 329: 405-416. PMID: 11210560, DOI: 10.1016/s0076-6879(01)29101-0.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAnimalsCell LineCell Membrane PermeabilityCoat Protein Complex IDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliFluorescent Antibody TechniqueGenetic VectorsGolgi ApparatusIntracellular MembranesPeptide FragmentsProtein BindingRecombinant Fusion ProteinsSpectrinConceptsADP-ribosylation factorGolgi membranesSpectrin peptidesPermeabilized cultured cellsBinding of spectrinCultured cell linesDifferent functional domainsSpectrin assemblySequence motifsRibosylation factorIndirect immunofluorescent microscopyFunctional domainsIntracellular distributionCultured cellsSpectrinΒIII spectrinImmunofluorescence analysisCell linesGolgiImmunofluorescent microscopyExperimental strategiesPeptidesMembraneCellsOrganelles
1994
Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2).
Lombardo C, Weed S, Kennedy S, Forget B, Morrow J. Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2). Journal Of Biological Chemistry 1994, 269: 29212-29219. PMID: 7961888, DOI: 10.1016/s0021-9258(19)62032-6.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainBeta II spectrinHomology domainSequence motifsBeta III-spectrinBrain spectrinGlutathione S-transferase fusion proteinRepeat 1S-transferase fusion proteinMembrane association domainNovel functional motifsCOOH-terminal domainG protein bindingDistinct sequence motifsBovine brain spectrinCOOH-terminal sequenceAssociation domainMembrane associationProtein 4.1Spectrin functionSequence comparisonPlasma membraneFunctional motifsRecombinant proteins