Abstract
Ankyrin repeats (ANKs) are one of the most abundant and conserved tandem repeats in various species. Ankyrin repeat domains (ARDs) have been recognized as protein–protein interaction modules. However, some ARDs were found to bind to specific lipids. The two ARD-containing proteins, ANK and KH domain-containing protein 1 (ANKHD1) and ankycorbin, were membrane-deforming proteins in the cellular membrane. The structural motifs of the ANKs stack together to form an elongated structure, predicted to be a curved conformation, for sensing the membrane curvature. Furthermore, ANKHD1 and ankycorbin have an adjacent amphipathic helix to the ANKs for the generation of membrane curvature and require self-assembly for their localization. Therefore these ARDs with the amphipathic helix act as membrane-deforming modules upon their self-assembly in the cell membrane. This chapter provides new insights into the membrane interaction and deformation properties of ANKs.
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