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

Jun Yan | Zendy; Qijie Li | Zendy; Aiping Mao | Zendy; MingMing Hu | Zendy; HongBing Shu | Zendy

Open Access

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

Author(s) -

Jun Yan,

Qijie Li,

Aiping Mao,

MingMing Hu,

HongBing Shu

Publication year - 2014

Publication title -

journal of molecular cell biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.825

H-Index - 62

eISSN - 1674-2788

pISSN - 1759-4685

DOI - 10.1093/jmcb/mju005

Subject(s) - irf3 , rig i , ubiquitin , gene knockdown , interferon , regulator , microbiology and biotechnology , biology , interferon regulatory factors , interferon type i , irf7 , transcription factor , tank binding kinase 1 , antiviral protein , signal transduction , innate immune system , virology , gene , rna , genetics , receptor , mitogen activated protein kinase kinase , protein kinase c

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.

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