HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I
| Autor: | Jing Li, Ting Ling, Liang-Guo Xu, Tao Xie, Jing-Ping Huang, Ya-Xian Yang, Sheng-Na Li |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
viruses Immunology chemical and pharmacologic phenomena Respirovirus Infections Sendai virus 03 medical and health sciences 0302 clinical medicine Humans Receptors Immunologic Molecular Biology Adaptor Proteins Signal Transducing Gene knockdown biology Chemistry RIG-I Binding protein Ubiquitination virus diseases Signal transducing adaptor protein RNA biochemical phenomena metabolism and nutrition biology.organism_classification Immunity Innate Cell biology HEK293 Cells 030104 developmental biology DEAD Box Protein 58 Signal transduction IRF3 Signal Transduction 030215 immunology |
| Zdroj: | Molecular Immunology. 134:62-71 |
| ISSN: | 0161-5890 |
| DOI: | 10.1016/j.molimm.2021.03.002 |
| Popis: | Retinoic acid-inducible gene I (RIG-I) plays a critical role in the recognition of intracytoplasmic viral RNA. Upon binding to the RNA of invading viruses, the activated RIG-I translocates to mitochondria, where it recruits adapter protein MAVS, causing a series of signaling cascades. In this study, we demonstrated that Hsp70 binding protein 1 (HSPBP1) promotes RIG-I-mediated signal transduction. The overexpression of HSPBP1 can increase the stability of RIG-I protein by inhibiting its K48-linked ubiquitination, and promote the activation of IRF3 and the production of IFN-β induced by Sendai virus. Knockdown and knockout of HSPBP1 leads to down-regulation of virus-induced RIG-I expression, inhibits IRF3 activation, and reduces the production of IFNB1. These results indicate that HSPBP1 positively regulates the antiviral signal pathway induced by inhibiting the K48-linked ubiquitination of RIG-I. |
| Databáze: | OpenAIRE |
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