REVIEW: Ankyrin: Structure, Properties, and Functions

M. A. Batrukova¹, V. L. Betin², A. M. Rubtsov¹, and O. D. Lopina^1*

¹Department of Biochemistry and ²Department of Bioorganic Chemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-3955; E-mail: odl@atpase.bio.msu.su

^* To whom correspondence should be addressed.

Received June 17, 1999; Revision received November 4, 1999

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Recent data on characteristics of the structure, functions, and main properties of ankyrins (proteins that are linkers between the spectrin-based cytoskeleton and integral membrane proteins) are summarized. The interactions of ankyrins with band-3 protein, P-type ATPases, ion channels, receptors, and protein kinase C are considered. The structure of ankyrin repeats that are often contained in other proteins (which are not classified with the ankyrin family) and ensure protein-protein interactions as well as interactions between proteins and nucleic acids is described in details. The mechanisms of regulation of the ability of ankyrins to interact with other proteins (alternative splicing and post-translational modification, including phosphorylation) are also considered.

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KEY WORDS: ankyrin, membrane spectrin-based cytoskeleton, integral membrane proteins

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