Abstract
The inner side of the red-cell membrane is laminated by a two-dimensional network of membrane proteins which include spectrin, actin and some other components1–4. After extraction of lipids and integral proteins from the membrane, this membrane skeleton can be visualized as a ball-shaped network consisting of twisted fibres1–4 and globular protrusions4; however, the assembly of the individual proteins in the membrane skeleton is not well understood. Spectrin can be eluted from the membrane in the form of dimers and tetramers5–8. Electron microscopic study with low-angle shadowing technique shows that spectrin dimers are two parallel strands of twisted fibres presumably representing bands 1 and 2 of spectrin9. Spectrin tetramers presumably formed by head-to-head associations of two dimers are twice as long9. In solution, the spectrin dimer–tetramer equilibrium depends on temperature and salt concentration7,8; however, it is not known whether the same equilibrium exists in the membrane and whether it affects the physical properties of the membrane, such as its structural stability and deformability. We now demonstrate that spectrin dimers and tetramers are in a reversible equilibrium in the membrane and that in physiological conditions this equilibrium favours spectrin tetramers. Furthermore, we show that transformation of spectrin tetramers to dimers, as induced by ghost incubation in hypotonic conditions, diminishes the structural stability of the Triton-insoluble membrane skeletons.
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Liu, SC., Palek, J. Spectrin tetramer–dimer equilibrium and the stability of erythrocyte membrane skeletons. Nature 285, 586–588 (1980). https://doi.org/10.1038/285586a0
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DOI: https://doi.org/10.1038/285586a0
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