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MAVS Ubiquitylation: Function, Mechanism, and Beyond
Hongliang Dong1,2, Jie Shen1,2,*
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1
Department of GI Surgery, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, Hubei, China
2
GI Cancer Research Institute, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, Hubei, China
*Correspondence: jieshen@tjh.tjmu.edu.cn (Jie Shen)
Front. Biosci. (Landmark Ed) 2024, 29(2), 72;
https://doi.org/10.31083/j.fbl2902072
Submitted: 30 October 2023 | Revised: 16 December 2023 | Accepted: 11 January 2024 | Published: 21 February 2024
Copyright: © 2024 The Author(s). Published by IMR Press.
This is an open access article under the CC BY 4.0 license.
Abstract
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.
Keywords
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
Funding
2023AFB118/Hubei Provincial Natural Science Foundation of China
2022B24/Science Foundation of Tongji Hospital
Figures
Fig. 1.