Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Kitamata, Manabu, Hanawa-Suetsugu, Kyoko, Maruyama, Kohei, Suetsugu, Shiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
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
_version_ 1783432001674543104
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
work_keys_str_mv AT kitamatamanabu membranedeformationabilityofankhd1isinvolvedintheearlyendosomeenlargement
AT hanawasuetsugukyoko membranedeformationabilityofankhd1isinvolvedintheearlyendosomeenlargement
AT maruyamakohei membranedeformationabilityofankhd1isinvolvedintheearlyendosomeenlargement
AT suetsugushiro membranedeformationabilityofankhd1isinvolvedintheearlyendosomeenlargement