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...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2023-08-01
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| Series: | Frontiers in Cellular and Infection Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcimb.2023.1205355/full |
| _version_ | 1797742163177504768 |
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| author | Yulu Zhang Yulu Zhang Yulu Zhang Yupei Yuan Yupei Yuan Lu Jiang Lu Jiang Yihan Liu Yihan Liu Leiliang Zhang Leiliang Zhang Leiliang Zhang |
| author_facet | Yulu Zhang Yulu Zhang Yulu Zhang Yupei Yuan Yupei Yuan Lu Jiang Lu Jiang Yihan Liu Yihan Liu Leiliang Zhang Leiliang Zhang Leiliang Zhang |
| author_sort | Yulu Zhang |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-12T14:37:02Z |
| format | Article |
| id | doaj.art-3801c972024b4f8d852a27b91a561832 |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-03-12T14:37:02Z |
| publishDate | 2023-08-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-3801c972024b4f8d852a27b91a5618322023-08-17T04:27:25ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882023-08-011310.3389/fcimb.2023.12053551205355The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinantYulu Zhang0Yulu Zhang1Yulu Zhang2Yupei Yuan3Yupei Yuan4Lu Jiang5Lu Jiang6Yihan Liu7Yihan Liu8Leiliang Zhang9Leiliang Zhang10Leiliang Zhang11Department of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University and Shandong Provincial Qianfoshan Hospital, Jinan, Shandong, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaDepartment of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University and Shandong Provincial Qianfoshan Hospital, Jinan, Shandong, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaRing 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.https://www.frontiersin.org/articles/10.3389/fcimb.2023.1205355/fullRNF213antimicrobial infectionubiquitinationlipid dropletscell autonomous immunity |
| spellingShingle | Yulu Zhang Yulu Zhang Yulu Zhang Yupei Yuan Yupei Yuan Lu Jiang Lu Jiang Yihan Liu Yihan Liu Leiliang Zhang Leiliang Zhang Leiliang Zhang The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant Frontiers in Cellular and Infection Microbiology RNF213 antimicrobial infection ubiquitination lipid droplets cell autonomous immunity |
| 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 | RNF213 antimicrobial infection ubiquitination lipid droplets cell autonomous immunity |
| url | https://www.frontiersin.org/articles/10.3389/fcimb.2023.1205355/full |
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