HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I.
HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I.
复制标题
DOI：
10.1016/j.molimm.2021.03.002
复制
发表时间：
2021-03
影响因子：
3.6
通讯作者：
Ya-Xian Yang;Jing-Ping Huang;Sheng‐Na Li;Jing Li;T. Ling;T. Xie;Liang-Guo Xu
中科院分区：
文献类型：
--
作者：
Ya-Xian Yang;Jing-Ping Huang;Sheng‐Na Li;Jing Li;T. Ling;T. Xie;Liang-Guo Xu
视黄酸诱导基因I （RIG-I）在胞浆内病毒RNA的识别中起关键作用。在与入侵病毒的RNA结合后，活化的RIG-I易位到线粒体，在那里招募适配蛋白MAVS，引起一系列信号级联反应。在这项研究中，我们证明了Hsp70结合蛋白1 （HSPBP1）促进rig - i介导的信号转导。HSPBP1过表达可通过抑制rig - 1蛋白k48连锁泛素化而提高其稳定性，促进仙台病毒诱导的IRF3的激活和IFN-β的产生。敲低和敲除HSPBP1导致病毒诱导的RIG-I表达下调，抑制IRF3的激活，减少IFNB1的产生。这些结果表明，HSPBP1通过抑制RIG-I的k48连锁泛素化而正向调节抗病毒信号通路。
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.