iScience (Jul 2019)

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

  • Manabu Kitamata,
  • Kyoko Hanawa-Suetsugu,
  • Kohei Maruyama,
  • Shiro Suetsugu

Journal volume & issue
Vol. 17
pp. 101 – 118

Abstract

Read online

Summary: 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. : Biological Sciences; Biochemistry; Molecular Biology; Membrane Architecture; Cell Biology Subject Areas: Biological Sciences, Biochemistry, Molecular Biology, Membrane Architecture, Cell Biology