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 distributionIdentification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta I sigma spectrin and associates with the Golgi apparatus.
Devarajan P, Stabach PR, Mann AS, Ardito T, Kashgarian M, Morrow JS. Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta I sigma spectrin and associates with the Golgi apparatus. Journal Of Cell Biology 1996, 133: 819-830. PMID: 8666667, PMCID: PMC2120834, DOI: 10.1083/jcb.133.4.819.Peer-Reviewed Original ResearchConceptsMDCK cell lysatesGolgi apparatusMDCK cellsBeta IDomain IPlasma membrane localizationTrans-Golgi networkPutative regulatory domainCell lysatesPolarized vesicle transportMembrane-associated proteinsCell cycle controlSubset of endosomesNovel ankyrinPolarity developmentVesicle transportMotif characteristicMembrane localizationRegulatory domainProtein microdomainsSequence comparisonAlternative transcriptsRepetitive domainSubconfluent MDCK cellsMembrane skeleton