Regulation of MAVS activation through post-translational modifications

Bingyu Liu; Chengjiang Gao

doi:10.1016/j.coi.2017.12.002

Regulation of MAVS activation through post-translational modifications

Curr Opin Immunol. 2018 Feb:50:75-81. doi: 10.1016/j.coi.2017.12.002. Epub 2017 Dec 12.

Authors

Bingyu Liu¹, Chengjiang Gao²

Affiliations

¹ State Key Laboratory of Microbial technology, Key Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, the School of Basic Medical Sciences, Shandong University, Jinan, Shandong 250012, China.
² State Key Laboratory of Microbial technology, Key Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, the School of Basic Medical Sciences, Shandong University, Jinan, Shandong 250012, China. Electronic address: cgao@sdu.edu.cn.

PMID: 29245018
DOI: 10.1016/j.coi.2017.12.002

Abstract

RLRs (including RIG-I and MDA5) are the main receptors that recognize cytoplasmic viral RNA. Upon binding of viral RNA, RIG-I and MDA5 recruit mitochondria-localized MAVS to activate the downstream antiviral signaling. MAVS forms prion-like aggregates on the mitochondria after virus infection. The regulatory mechanisms for MAVS activation have been defined in various studies. Here, we summarize the recent advances about MAVS roles in antiviral immunity, discuss the regulation of MAVS activation, and suggest interesting areas for future research.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adaptor Proteins, Signal Transducing / chemistry
Adaptor Proteins, Signal Transducing / genetics*
Adaptor Proteins, Signal Transducing / metabolism*
Animals
Gene Expression Regulation*
Humans
Phosphorylation
Protein Aggregates
Protein Binding
Protein Processing, Post-Translational*
Structure-Activity Relationship
Transcriptional Activation*
Ubiquitination

Substances

Adaptor Proteins, Signal Transducing
MAVS protein, human
Protein Aggregates