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Full-length sequence of the cDNA for human erythroid beta-spectrin.
Open accessAbstract
Spectrin is the major molecular consituent of the red cell membrane skeleton. We have isolated overlapping human erythroid beta-spectrin cDNA clones and determined 6773 base pairs of contiguous nucleotide sequence. This includes the entire coding sequence of beta-spectrin. The sequence translates into a 2137 amino acid, 246-kDa peptide. beta-Spectrin is found to consist of three distinct domains. Domain I, at the N terminus, is a 272-amino acid region lacking resemblance to the spectrin repetitive motif. Sequences in this region exhibit striking sequence homology, at both nucleotide and amino acid levels, to the N-terminal "actin-binding" domains of alpha-actinin and dystrophin. Between residues 51 and 270 there is 55% amino acid identity to human dystrophin, with only four single amino acid gaps in alignment. Domain II consists of 17 spectrin repeats. Several sequence variations are observed in typical repeat structure. Homology to alpha-actinin extends beyond domain I into the N-terminal portion of domain II. Domain III, 52 amino acid residues at the C terminus, does not adhere to the spectrin repeat motif. Combining knowledge of spectrin primary structure with previously reported functional studies, it is possible to make several inferences regarding structure/function relationships within the beta-spectrin molecule.
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Cites
Dystrophin: the protein product of the Duchenne muscular dystrophy locus
Hoffman, E. P., Brown, R. H., & Kunkel, L. M. (1987) · Cell · doi:10.1016/0092-8674(87)90579-4 · Cited by 4,693
Cited by
Spectrin and Ankyrin-Based Pathways: Metazoan Inventions for Integrating Cells Into Tissues
Bennett, V., & Baines, A. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.3.1353 · Cited by 930
Hartwig, J. H., & Kwiatkowski, D. J. (1991) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(91)90170-4 · Cited by 287
Berghs, S., Aggujaro, D., Dirkx, R., Maksimova, E., Stabach, P., Hermel, J.-M., Zhang, J.-P., Philbrick, W., Slepnev, V., Ort, T., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.5.985 · Cited by 275
A Novel Brain-Specific Isoform of β Spectrin: Isolation and Its Interaction with Munc13
Sakaguchi, G., Orita, S., Naito, A., Maeda, M., Igarashi, H., Sasaki, T., & Takai, Y. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9067 · Cited by 58
Effects of dextran on the self-association of human spectrin
Lindner, R., & Ralston, G. (1995) · Biophysical Chemistry · doi:10.1016/0301-4622(95)00063-4 · Cited by 46
Metadata
- Authors
- Winkelmann, J. C., Chang, J. G., Tse, W. T., Scarpa, A. L., Marchesi, V. T., & Forget, B. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-07
- Volume
- 265
- Issue
- 20
- Pages
- 11827-11832
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1489771083
- Cited by
- 234
- References
- 1
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Winkelmann, J. C., Chang, J. G., Tse, W. T., Scarpa, A. L., Marchesi, V. T., & Forget, B. G. (1990). Full-length sequence of the cDNA for human erythroid beta-spectrin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)38473-x
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