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
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 ResearchConceptsBeta 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