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Ankyrin is fatty acid acylated in erythrocytes

Staufenbiel, Matthias and Lazarides, Elias (1986) Ankyrin is fatty acid acylated in erythrocytes. Proceedings of the National Academy of Sciences of the United States of America, 83 (2). pp. 318-322. ISSN 0027-8424. PMCID PMC322849. doi:10.1073/pnas.83.2.318.

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Ankyrin is a peripheral membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane. We show that [3H]palmitic acid is incorporated into ankyrin in vivo. The majority of the 3H-labeled fatty acid is covalently bound to the polypeptide, as it cannot be removed by strong detergents or by chloroform/methanol extraction but is labile to alkaline hydrolysis. The binding of fatty acid occurs predominantly after the assembly of ankyrin onto the membrane skeleton, since it continues when protein synthesis is inhibited with emetine. Fatty acid acylation of ankyrin is constitutive in erythroid cells throughout chicken embryo development. It also occurs in mature avian and mammalian erythrocytes suggesting that the fatty acid bound to ankyrin turns over more rapidly than the polypeptide. Fatty acid acylation of assembled ankyrin may modulate the interaction of ankyrin with the plasma membrane. It may also provide a mechanism by which the membrane skeleton influences the organization of the lipid bilayer.

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Additional Information:© 1986 by the National Academy of Sciences. Communicated by Howard C. Berg, September 19, 1985. We thank Drs. Horst Hinssen, John Cox, and John Ngai for their comments on the manuscript. This work was supported by grants from the National Institutes of Health, National Science Foundation, and Muscular Dystrophy Association. M.S. was also supported by a Cancer Research Campaign International Fellowship awarded by the International Union Against Cancer and a Senior Investigatorship of the American Heart Association, Greater Los Angeles Affiliate.
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Muscular Dystrophy AssociationUNSPECIFIED
International Union Against CancerUNSPECIFIED
American Heart Association, Greater Los Angeles AffiliateUNSPECIFIED
Issue or Number:2
PubMed Central ID:PMC322849
Record Number:CaltechAUTHORS:STApnas86
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:11664
Deposited By: Archive Administrator
Deposited On:17 Sep 2008 20:54
Last Modified:08 Nov 2021 22:01

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