ArticleThe Journal of cell biology1987
Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 52 citations in OpenAlex.
- Spectrin Breakdown Products (SBDPs) as Potential Biomarkers for Neurodegenerative Diseases.Current translational geriatrics and experimental gerontology reports · 2012Article
- The actin binding domain of βI-spectrin regulates the morphological and functional dynamics of dendritic spines.PloS one · 2011Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- Immunolocalization of protein 4.1B in the rat digestive system.Journal of molecular histology · 2004Article
- The spectrin skeleton: from red cells to brain.The Journal of clinical investigation · 1991Review
- 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 · 1990Article
- Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.The Journal of cell biology · 1989Article
- Characterization and cytoskeletal association of a major cell surface glycoprotein, GP 140, in human neutrophils.The Journal of clinical investigation · 1989Article
- Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.The Journal of cell biology · 1989Article
- Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.The Journal of cell biology · 1987Article
- Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border.The American journal of pathology · 1987Article
- Drosophilia spectrin. I. Characterization of the purified protein.The Journal of cell biology · 1987Article
- Drosophila spectrin. II. Conserved features of the alpha-subunit are revealed by analysis of cDNA clones and fusion proteins.The Journal of cell biology · 1987Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The ability of protein 4.1 to stimulate the binding of spectrin to F-actin has been compared by cosedimentation analysis for three avian (erythrocyte, brain, and brush border) and two mammalian (erythrocyte and brain) spectrin isoforms. Human erythroid protein 4.1 stimulated actin binding of all spectrins except the brush border isoform (TW 260/240). These results suggested that the beta subunit determined the protein 4.1 sensitivity of the heterodimer, since all avian alpha subunits are encoded by a single gene. Tissue-specific posttranslational modification of the alpha subunit was excluded by examining the properties of hybrid spectrins composed of the purified alpha subunit from avian erythrocyte or brush border spectrin and the beta subunit of human erythrocyte spectrin. A hybrid composed of avian brush border alpha and human erythroid beta spectrin ran on nondenaturing gels as a discrete band, migrating near human erythroid spectrin tetramers. The actin-binding activity of this hybrid was stimulated by protein 4.1, while either chain alone was devoid of activity. Therefore, although both subunits were required for actin binding, the sensitivity of the spectrin-actin interaction to protein 4.1 is a property uniquely bestowed on the heterodimer by the beta subunit. The singular insensitivity of brush border spectrin to stimulation by erythroid protein 4.1 was also consistent with the absence of proteins in avian intestinal epithelial cells which were immunoreactive with polyclonal antisera sensitive to all of the known avian and human erythroid 4.1 isoforms.
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