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E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses

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  • Yinjing Song

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Lihua Lai

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Zhenlu Chong

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Jia He

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Yuanyuan Zhang

    (The Children’s Hospital, Zhejiang University School of Medicine)

  • Yue Xue

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Yiwei Xie

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Songchang Chen

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Ping Dong

    (Zhejiang University School of Medicine)

  • Luoquan Chen

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Zhimin Chen

    (The Children’s Hospital, Zhejiang University School of Medicine)

  • Feng Dai

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Xiaopeng Wan

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Peng Xiao

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Xuetao Cao

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China
    Chinese Academy of Medical Sciences)

  • Yang Liu

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

  • Qingqing Wang

    (Institute of Immunology, Zhejiang University School of Medicine, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China)

Abstract

Viruses can escape from host recognition by degradation of RIG-I or interference with the RIG-I signalling to establish persistent infections. However, the mechanisms by which host cells stabilize RIG-I protein for avoiding its degradation are largely unknown. We report here that, upon virus infection, the E3 ubiquitin ligase FBXW7 translocates from the nucleus into the cytoplasm and stabilizes RIG-I. FBXW7 interacts with SHP2 and mediates the degradation and ubiquitination of SHP2, thus disrupting the SHP2/c-Cbl complex, which mediates RIG-I degradation. When infected with VSV or influenza A virus, FBXW7 conditional knockout mice (Lysm+FBXW7f/f) show impaired antiviral immunity. FBXW7-deficient macrophages have decreased RIG-I protein levels and type-I interferon signalling. Furthermore, PBMCs from RSV-infected children have reduced FBXW7 mRNA levels. Our results identify FBXW7 as an important interacting partner for RIG-I. These findings provide insights into the function of FBXW7 in antiviral immunity and its related clinical significance.

Suggested Citation

  • Yinjing Song & Lihua Lai & Zhenlu Chong & Jia He & Yuanyuan Zhang & Yue Xue & Yiwei Xie & Songchang Chen & Ping Dong & Luoquan Chen & Zhimin Chen & Feng Dai & Xiaopeng Wan & Peng Xiao & Xuetao Cao & Y, 2017. "E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses," Nature Communications, Nature, vol. 8(1), pages 1-14, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14654
    DOI: 10.1038/ncomms14654
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