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iScience. 2019 Jul 26;17:101-118. doi: 10.1016/j.isci.2019.06.020. Epub 2019 Jun 18.

Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement.

Author information

1
Graduate School of Science and Technology, Nara Institute of Science and Technology, Ikoma 630-0192, Japan.
2
Graduate School of Science and Technology, Nara Institute of Science and Technology, Ikoma 630-0192, Japan. Electronic address: suetsugu@bs.naist.jp.

Abstract

Ankyrin-repeat domains (ARDs) are conserved in large numbers of proteins. ARDs are composed of various numbers of ankyrin repeats (ANKs). ARDs often adopt curved structures reminiscent of the Bin-Amphiphysin-Rvs (BAR) domain, which is the dimeric scaffold for membrane tubulation. BAR domains sometimes have amphipathic helices for membrane tubulation and vesiculation. However, it is unclear whether ARD-containing proteins exhibit similar membrane deformation properties. We found that the ARD of ANK and KH domain-containing protein 1 (ANKHD1) dimerize and deform membranes into tubules and vesicles. Among 25 ANKs of ANKHD1, the first 15 ANKs can form a dimer and the latter 10 ANKs enable membrane tubulation and vesiculation through an adjacent amphipathic helix and a predicted curved structure with a positively charged surface, analogous to BAR domains. Knockdown and localization of ANKHD1 suggested its involvement in the negative regulation of early endosome enlargement owing to its membrane vesiculation.

KEYWORDS:

Biochemistry; Biological Sciences; Cell Biology; Membrane Architecture; Molecular Biology

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