Unit of Molecular Signal Transduction in Inflammation, Department for Molecular Biomedical Research, VIB, Ghent, Belgium.
Microbiol Mol Biol Rev. 2012 Mar;76(1):33-45. doi: 10.1128/MMBR.05012-11.
Detection of viruses by the innate immune system involves the action of specialized pattern recognition receptors. Intracellular RIG-I receptors sense the presence of viral nucleic acids in infected cells and trigger signaling pathways that lead to the production of proinflammatory and antiviral proteins. Over the past few years, posttranslational modification of RIG-I and downstream signaling proteins by different types of ubiquitination has been found to be a key event in the regulation of RIG-I-induced NF-κB and interferon regulatory factor 3 (IRF3) activation. Multiple ubiquitin ligases, deubiquitinases, and ubiquitin binding scaffold proteins contribute to both positive and negative regulation of the RIG-I-induced antiviral immune response. A better understanding of the function and activity of these proteins might eventually lead to the development of novel therapeutic approaches for management of viral diseases.
先天免疫系统通过特定的模式识别受体来检测病毒。细胞内的 RIG-I 受体可以感知感染细胞中病毒核酸的存在，并启动信号通路，导致促炎和抗病毒蛋白的产生。在过去的几年中，RIG-I 和下游信号蛋白的翻译后修饰，如不同类型的泛素化，已被发现是调节 RIG-I 诱导的 NF-κB 和干扰素调节因子 3 (IRF3) 激活的关键事件。多种泛素连接酶、去泛素化酶和泛素结合支架蛋白参与了 RIG-I 诱导的抗病毒免疫反应的正调控和负调控。对这些蛋白质的功能和活性的更好理解可能最终导致开发新的治疗方法来管理病毒疾病。
