Membrane-deformation ability of ANKHD1 is involved in the early endosome enlargement

• Kitamata, Manabu

• Hanawa-Suetsugu, Kyoko

• Maruyama, Kohei

• Suetsugu, Shiro

抄録

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 ankyrin repeat and KH domain-containing protein 1 (ANKHD1) dimerizes and deforms 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.

収録刊行物

• iScience

  iScience 17 101-118, 2019-07-26

  Elsevier (Cell Press)

キーワード

• Multidisciplinary

詳細情報

• CRID: 1050014359399341312
• NII論文ID: 120006723244
• ISSN: 25890042
• DOI: 10.1016/j.isci.2019.06.020
• HANDLE: 10061/13377
• Web Site: https://naist.repo.nii.ac.jp/records/9236
• Web Site: https://api.elsevier.com/content/article/PII:S2589004219302032?httpAccept=text/xml
• Web Site: https://api.elsevier.com/content/article/PII:S2589004219302032?httpAccept=text/plain
• 本文言語コード: en
• 資料種別: journal article
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