MAVS Ubiquitylation: Function, Mechanism, and Beyond
The mitochondrial antiviral-signaling protein (MAVS), a core adaptor protein in the retinoic-acid-inducible gene-I-like receptors (RLRs)-MAVS pathway, has been demonstrated to play an important role in antiviral immune response and tumor immunology. Previous studies revealed that ubiquitylation is a...
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| Format: | Article |
| Language: | English |
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IMR Press
2024-02-01
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| Series: | Frontiers in Bioscience-Landmark |
| Subjects: | |
| Online Access: | https://www.imrpress.com/journal/FBL/29/2/10.31083/j.fbl2902072 |
| _version_ | 1827572751080095744 |
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| author | Hongliang Dong Jie Shen |
| author_facet | Hongliang Dong Jie Shen |
| author_sort | Hongliang Dong |
| collection | DOAJ |
| description | The mitochondrial antiviral-signaling protein (MAVS), a core adaptor protein in the retinoic-acid-inducible gene-I-like receptors (RLRs)-MAVS pathway, has been demonstrated to play an important role in antiviral immune response and tumor immunology. Previous studies revealed that ubiquitylation is a key mechanism in the regulation of the RLRs-MAVS axis and immune response. Multiple E3 ubiquitin ligases and deubiquitinating enzymes control MAVS ubiquitylation and changes in MAVS function. In this review, we summarize the biological function of ubiquitylation in MAVS-related signaling and provide new insight into immunotherapy approaches that target MAVS. |
| first_indexed | 2024-03-07T19:21:59Z |
| format | Article |
| id | doaj.art-84941d78eada4d149d717c633e620f12 |
| institution | Directory Open Access Journal |
| issn | 2768-6701 |
| language | English |
| last_indexed | 2024-03-07T19:21:59Z |
| publishDate | 2024-02-01 |
| publisher | IMR Press |
| record_format | Article |
| series | Frontiers in Bioscience-Landmark |
| spelling | doaj.art-84941d78eada4d149d717c633e620f122024-02-29T09:53:16ZengIMR PressFrontiers in Bioscience-Landmark2768-67012024-02-012927210.31083/j.fbl2902072S2768-6701(24)01205-XMAVS Ubiquitylation: Function, Mechanism, and BeyondHongliang Dong0Jie Shen1Department of GI Surgery, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, Hubei, ChinaDepartment of GI Surgery, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, Hubei, ChinaThe mitochondrial antiviral-signaling protein (MAVS), a core adaptor protein in the retinoic-acid-inducible gene-I-like receptors (RLRs)-MAVS pathway, has been demonstrated to play an important role in antiviral immune response and tumor immunology. Previous studies revealed that ubiquitylation is a key mechanism in the regulation of the RLRs-MAVS axis and immune response. Multiple E3 ubiquitin ligases and deubiquitinating enzymes control MAVS ubiquitylation and changes in MAVS function. In this review, we summarize the biological function of ubiquitylation in MAVS-related signaling and provide new insight into immunotherapy approaches that target MAVS.https://www.imrpress.com/journal/FBL/29/2/10.31083/j.fbl2902072mavsubiquitylationsumoylationring-finger type e3 ligasehect e3 ligaseu-box type e3 ligasesumo e3 ligasevirus-derived proteins function as e3 ligasede-ubiquitinase |
| spellingShingle | Hongliang Dong Jie Shen MAVS Ubiquitylation: Function, Mechanism, and Beyond Frontiers in Bioscience-Landmark mavs ubiquitylation sumoylation ring-finger type e3 ligase hect e3 ligase u-box type e3 ligase sumo e3 ligase virus-derived proteins function as e3 ligase de-ubiquitinase |
| title | MAVS Ubiquitylation: Function, Mechanism, and Beyond |
| title_full | MAVS Ubiquitylation: Function, Mechanism, and Beyond |
| title_fullStr | MAVS Ubiquitylation: Function, Mechanism, and Beyond |
| title_full_unstemmed | MAVS Ubiquitylation: Function, Mechanism, and Beyond |
| title_short | MAVS Ubiquitylation: Function, Mechanism, and Beyond |
| title_sort | mavs ubiquitylation function mechanism and beyond |
| topic | mavs ubiquitylation sumoylation ring-finger type e3 ligase hect e3 ligase u-box type e3 ligase sumo e3 ligase virus-derived proteins function as e3 ligase de-ubiquitinase |
| url | https://www.imrpress.com/journal/FBL/29/2/10.31083/j.fbl2902072 |
| work_keys_str_mv | AT hongliangdong mavsubiquitylationfunctionmechanismandbeyond AT jieshen mavsubiquitylationfunctionmechanismandbeyond |