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Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state
Moyamoya disease is an idiopathic human cerebrovascular disorder that is characterized by progressive stenosis and abnormal collateral vessels. We recently identified mysterin/RNF213 as its first susceptibility gene, which encodes a 591-kDa protein containing enzymatically active P-loop ATPase and u...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3963067/ https://www.ncbi.nlm.nih.gov/pubmed/24658080 http://dx.doi.org/10.1038/srep04442 |
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author | Morito, Daisuke Nishikawa, Kouki Hoseki, Jun Kitamura, Akira Kotani, Yuri Kiso, Kazumi Kinjo, Masataka Fujiyoshi, Yoshinori Nagata, Kazuhiro |
author_facet | Morito, Daisuke Nishikawa, Kouki Hoseki, Jun Kitamura, Akira Kotani, Yuri Kiso, Kazumi Kinjo, Masataka Fujiyoshi, Yoshinori Nagata, Kazuhiro |
author_sort | Morito, Daisuke |
collection | PubMed |
description | Moyamoya disease is an idiopathic human cerebrovascular disorder that is characterized by progressive stenosis and abnormal collateral vessels. We recently identified mysterin/RNF213 as its first susceptibility gene, which encodes a 591-kDa protein containing enzymatically active P-loop ATPase and ubiquitin ligase domains and is involved in proper vascular development in zebrafish. Here we demonstrate that mysterin further contains two tandem AAA+ ATPase modules and forms huge ring-shaped oligomeric complex. AAA+ ATPases are known to generally mediate various biophysical and mechanical processes with the characteristic ring-shaped structure. Fluorescence correlation spectroscopy and biochemical evaluation suggested that mysterin dynamically changes its oligomeric forms through ATP/ADP binding and hydrolysis cycles. Thus, the moyamoya disease-associated gene product is a unique protein that functions as ubiquitin ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. |
format | Online Article Text |
id | pubmed-3963067 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-39630672014-03-25 Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state Morito, Daisuke Nishikawa, Kouki Hoseki, Jun Kitamura, Akira Kotani, Yuri Kiso, Kazumi Kinjo, Masataka Fujiyoshi, Yoshinori Nagata, Kazuhiro Sci Rep Article Moyamoya disease is an idiopathic human cerebrovascular disorder that is characterized by progressive stenosis and abnormal collateral vessels. We recently identified mysterin/RNF213 as its first susceptibility gene, which encodes a 591-kDa protein containing enzymatically active P-loop ATPase and ubiquitin ligase domains and is involved in proper vascular development in zebrafish. Here we demonstrate that mysterin further contains two tandem AAA+ ATPase modules and forms huge ring-shaped oligomeric complex. AAA+ ATPases are known to generally mediate various biophysical and mechanical processes with the characteristic ring-shaped structure. Fluorescence correlation spectroscopy and biochemical evaluation suggested that mysterin dynamically changes its oligomeric forms through ATP/ADP binding and hydrolysis cycles. Thus, the moyamoya disease-associated gene product is a unique protein that functions as ubiquitin ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. Nature Publishing Group 2014-03-24 /pmc/articles/PMC3963067/ /pubmed/24658080 http://dx.doi.org/10.1038/srep04442 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/3.0/ This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Article Morito, Daisuke Nishikawa, Kouki Hoseki, Jun Kitamura, Akira Kotani, Yuri Kiso, Kazumi Kinjo, Masataka Fujiyoshi, Yoshinori Nagata, Kazuhiro Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state |
title | Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state |
title_full | Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state |
title_fullStr | Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state |
title_full_unstemmed | Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state |
title_short | Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state |
title_sort | moyamoya disease-associated protein mysterin/rnf213 is a novel aaa+ atpase, which dynamically changes its oligomeric state |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3963067/ https://www.ncbi.nlm.nih.gov/pubmed/24658080 http://dx.doi.org/10.1038/srep04442 |
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