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J Mol Cell Biol. 2014 Apr;6(2):154-63. doi: 10.1093/jmcb/mju005.

TRIM4 modulates type I interferon induction and cellular antiviral response by targeting RIG-I for K63-linked ubiquitination.

Author information

1
College of Life Sciences, Wuhan University, Wuhan 430072, China.

Abstract

RIG-I is a pivotal cytoplasmic sensor that recognizes different species of viral RNAs. This recognition leads to activation of the transcription factors NF-κB and IRF3, which collaborate to induce type I interferons (IFNs) and innate antiviral response. In this study, we identified the TRIM family protein TRIM4 as a positive regulator of RIG-I-mediated IFN induction. Overexpression of TRIM4 potentiated virus-triggered activation of IRF3 and NF-κB, as well as IFN-β induction, whereas knockdown of TRIM4 had opposite effects. Mechanistically, TRIM4 associates with RIG-I and targets it for K63-linked polyubiquitination. Our findings demonstrate that TRIM4 is an important regulator of the virus-induced IFN induction pathways by mediating RIG-I for K63-linked ubiquitination.

KEYWORDS:

RIG-I; TRIM4; antiviral response; type I interferon; ubiquitination

PMID:
24755855
DOI:
10.1093/jmcb/mju005
[Indexed for MEDLINE]

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