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Mol Cell Biol. 1987 August; 7(8): 2981-2984
Max-Planck-Institut für Zellbiologie, Abteilung Traub, Ladenburg bei Heidelberg, Federal Republic of Germany.
ABSTRACT
The membrane skeletal protein ankyrin was shown to be continuously acylated and deacylated with long-chain fatty acids in mature erythrocytes. At least a fraction of the lipid bound to ankyrin turned over rapidly (half-life, approximately 50 min) compared with the polypeptide backbone, which was stable throughout the erythrocyte life. This indicates a regulatory significance of the fatty acid modification for the function of ankyrin.
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