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The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant
Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space. Missense mutations in this gene have been found to be more prevalent in pat...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10465799/ https://www.ncbi.nlm.nih.gov/pubmed/37655297 http://dx.doi.org/10.3389/fcimb.2023.1205355 |
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author | Zhang, Yulu Yuan, Yupei Jiang, Lu Liu, Yihan Zhang, Leiliang |
author_facet | Zhang, Yulu Yuan, Yupei Jiang, Lu Liu, Yihan Zhang, Leiliang |
author_sort | Zhang, Yulu |
collection | PubMed |
description | Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space. Missense mutations in this gene have been found to be more prevalent in patients with moyamoya disease compared with that in healthy individuals. Understanding the molecular function of RNF213 could provide insights into moyamoya disease. RNF213 contains a C3HC4-type RING finger domain with an E3 ubiquitin ligase domain and six AAA+ adenosine triphosphatase (ATPase) domains. It is the only known protein with both AAA+ ATPase and ubiquitin ligase activities. Recent studies have highlighted the role of RNF213 in fighting against microbial infections, including viruses, parasites, bacteria, and chlamydiae. This review aims to summarize the recent research progress on the mechanisms of RNF213 in pathogenic infections, which will aid researchers in understanding the antimicrobial role of RNF213. |
format | Online Article Text |
id | pubmed-10465799 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-104657992023-08-31 The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant Zhang, Yulu Yuan, Yupei Jiang, Lu Liu, Yihan Zhang, Leiliang Front Cell Infect Microbiol Cellular and Infection Microbiology Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space. Missense mutations in this gene have been found to be more prevalent in patients with moyamoya disease compared with that in healthy individuals. Understanding the molecular function of RNF213 could provide insights into moyamoya disease. RNF213 contains a C3HC4-type RING finger domain with an E3 ubiquitin ligase domain and six AAA+ adenosine triphosphatase (ATPase) domains. It is the only known protein with both AAA+ ATPase and ubiquitin ligase activities. Recent studies have highlighted the role of RNF213 in fighting against microbial infections, including viruses, parasites, bacteria, and chlamydiae. This review aims to summarize the recent research progress on the mechanisms of RNF213 in pathogenic infections, which will aid researchers in understanding the antimicrobial role of RNF213. Frontiers Media S.A. 2023-08-15 /pmc/articles/PMC10465799/ /pubmed/37655297 http://dx.doi.org/10.3389/fcimb.2023.1205355 Text en Copyright © 2023 Zhang, Yuan, Jiang, Liu and Zhang https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cellular and Infection Microbiology Zhang, Yulu Yuan, Yupei Jiang, Lu Liu, Yihan Zhang, Leiliang The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant |
title | The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant |
title_full | The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant |
title_fullStr | The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant |
title_full_unstemmed | The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant |
title_short | The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant |
title_sort | emerging role of e3 ubiquitin ligase rnf213 as an antimicrobial host determinant |
topic | Cellular and Infection Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10465799/ https://www.ncbi.nlm.nih.gov/pubmed/37655297 http://dx.doi.org/10.3389/fcimb.2023.1205355 |
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