Abstract
The formation of a high-molecular weight complex between spectrin and F-actin depends on the presence of a third cytoskeletal constituent, protein 4.1. Electron microscopy shows that in this ternary complex the actin filaments are linked by bridges, which have the appearance of spectrin. The spectrin must be in the tetrameric state for such bridges to form: the dimer is evidently univalent, for it binds but forms no cross-links. G-actin also fails to form extended complexes. It is inferred that in the native cytoskeleton the spectrin is tetrameric and associated with 4.1 and probably oligomers of actin.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Mohandas, N. & Shohet, S. B. Curr. Topics Haemat. 1, 72–150 (1978).
Hainfeld, J. F. & Steck, T. L. J. supramolec. Struct. 6, 301–311 (1977).
Yu, J., Fischmann, D. A. & Steck, T. L. J. supramolec. Struct. 1, 233–248 (1973).
Pinder, J. C., Bray, D. & Gratzer, W. B. Nature 270, 752–754 (1977).
Lux, S. E. & John, K. M. in Cell Shape and Surface Architecture (eds Revel, J. P., Henning, U. & Fox, C. F.) 481–491 (Liss, New York, 1977).
Fairbanks, G., Steck, J. L. & Wallach, D. F. H. Biochemistry 10, 2606–2617 (1971).
Pinder, J. C., Bray, D. & Gratzer, W. B. Nature 258, 765–766 (1975).
Sheetz, M. P., Painter, R. G. & Singer, S. J. Biochemistry 15, 4486–4492 (1976).
Spudich, J. A. & Watt, S. J. J. biol. Chem. 246, 4866–4871 (1971).
Shotton, D., Burke, B. & Branton, D. Biochim. biophys. Acta 536, 313–317 (1978).
Ungewickell, E. & Gratzer, W. B. Eur. J. Biochem. 88, 379–385 (1978).
Tilney, L. F. & Detmers, L. G. J. Cell Biol. 66, 508–520 (1975).
Cohen, C. M. & Branton, D. Nature 279, 163–165 (1979).
Puszkin, S., Maimon, J. & Puszkin, E. Biochim. biophys. Acta 513, 205–220 (1978).
Brenner, S. L. & Korn, E. D. Fedn Proc. 38, 469 (1979).
Pinder, J. C., Ungewickell, E., Bray, D. & Gratzer, W. B. J. supramolec. Struct. 8, 439–445 (1978).
Wang, K. & Richards, F. M. J. biol. Chem. 250, 6622–6626 (1975).
Wolfe, L. C. & Lux, S. E. J. biol. Chem. 253, 3336–3342 (1978).
Birchmeier, W. & Singer, S. J. J. Cell Biol. 73, 647–659 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ungewickell, E., Bennett, P., Calvert, R. et al. In vitro formation of a complex between cytoskeletal proteins of the human erythrocyte. Nature 280, 811–814 (1979). https://doi.org/10.1038/280811a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/280811a0
This article is cited by
-
Differential dielectroscopic data on the relation of erythrocyte membrane skeleton to erythrocyte deformability and flicker
European Biophysics Journal (2021)
-
Human erythrocytes: cytoskeleton and its origin
Cellular and Molecular Life Sciences (2020)
-
Spectrin is a mechanoresponsive protein shaping fusogenic synapse architecture during myoblast fusion
Nature Cell Biology (2018)
-
The spectrin–ankyrin–4.1–adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life
Protoplasma (2010)
-
Reversible erythrocyte skeleton destabilization is modulated by beta-spectrin phosphorylation in childhood leukemia
Leukemia (2001)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.