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Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement
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 sometim...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6606961/ https://www.ncbi.nlm.nih.gov/pubmed/31255983 http://dx.doi.org/10.1016/j.isci.2019.06.020 |
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author | Kitamata, Manabu Hanawa-Suetsugu, Kyoko Maruyama, Kohei Suetsugu, Shiro |
author_facet | Kitamata, Manabu Hanawa-Suetsugu, Kyoko Maruyama, Kohei Suetsugu, Shiro |
author_sort | Kitamata, Manabu |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6606961 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-66069612019-07-15 Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement Kitamata, Manabu Hanawa-Suetsugu, Kyoko Maruyama, Kohei Suetsugu, Shiro iScience Article 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. Elsevier 2019-06-18 /pmc/articles/PMC6606961/ /pubmed/31255983 http://dx.doi.org/10.1016/j.isci.2019.06.020 Text en © 2019 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Kitamata, Manabu Hanawa-Suetsugu, Kyoko Maruyama, Kohei Suetsugu, Shiro Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement |
title | Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement |
title_full | Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement |
title_fullStr | Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement |
title_full_unstemmed | Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement |
title_short | Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement |
title_sort | membrane-deformation ability of ankhd1 is involved in the early endosome enlargement |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6606961/ https://www.ncbi.nlm.nih.gov/pubmed/31255983 http://dx.doi.org/10.1016/j.isci.2019.06.020 |
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