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O- Linked N-Acetylglucosamine Modification of Mitochondrial Antiviral Signaling Protein Regulates Antiviral Signaling by Modulating Its Activity

Authors
 Junghwa Seo  ;  Yun Soo Park  ;  Tae Hyun Kweon  ;  Jingu Kang  ;  Seongjin Son  ;  Han Byeol Kim  ;  Yu Ri Seo  ;  Min Jueng Kang  ;  Eugene C Yi  ;  Yong-Ho Lee  ;  Jin-Hong Kim  ;  Boyoun Park  ;  Won Ho Yang  ;  Jin Won Cho 
Citation
 FRONTIERS IN IMMUNOLOGY, Vol.11 : 589259, 2021-02 
Journal Title
 FRONTIERS IN IMMUNOLOGY 
Issue Date
2021-02
Keywords
O-linked N-Acetylglucosamine (O-GlcNAc) ; RIG-I-like receptors signaling ; host defense mechanism ; innate immunity ; mitochondrial antiviral signaling protein
Abstract
Post-translational modifications, including O-GlcNAcylation, play fundamental roles in modulating cellular events, including transcription, signal transduction, and immune signaling. Several molecular targets of O-GlcNAcylation associated with pathogen-induced innate immune responses have been identified; however, the direct regulatory mechanisms linking O-GlcNAcylation with antiviral RIG-I-like receptor signaling are not fully understood. In this study, we found that cellular levels of O-GlcNAcylation decline in response to infection with Sendai virus. We identified a heavily O-GlcNAcylated serine-rich region between amino acids 249-257 of the mitochondrial antiviral signaling protein (MAVS); modification at this site disrupts MAVS aggregation and prevents MAVS-mediated activation and signaling. O-GlcNAcylation of the serine-rich region of MAVS also suppresses its interaction with TRAF3; this prevents IRF3 activation and production of interferon-β. Taken together, these results suggest that O-GlcNAcylation of MAVS may be a master regulatory event that promotes host defense against RNA viruses.
Files in This Item:
T202100550.pdf Download
DOI
10.3389/fimmu.2020.589259
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers
Yonsei Authors
Lee, Yong Ho(이용호) ORCID logo https://orcid.org/0000-0002-6219-4942
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/182182
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