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首页> 外文期刊>Molecular and Cellular Biology >Interferon Regulatory Factor 7 Is Activated by a Viral Oncoprotein through RIP-Dependent Ubiquitination
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Interferon Regulatory Factor 7 Is Activated by a Viral Oncoprotein through RIP-Dependent Ubiquitination

机译：干扰素调节因子7被病毒癌蛋白通过RIP依赖性泛素激活。

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As a key mediator of type I interferon (IFN) (IFN-α/β) responses, IFN regulatory factor 7 (IRF7) is essential to host immune defenses. Activation of IRF7 generally requires virus-induced C-terminal phosphorylation, which leads to its nuclear accumulation and activation of target genes. Here we use the Epstein-Barr virus (EBV) oncoprotein LMP1, which activates IRF7, to identify factors involved in IRF7 activation. We demonstrate for the first time that RIP activates IRF7 and that RIP and IRF7 interact under physiological conditions in EBV-positive Burkitt's lymphoma cells. We provide evidence that both RIP and IRF7 are ubiquitinated in these cells and that IRF7 preferentially interacts with ubiquitinated RIP. RIP is required for full activation of IRF7 by LMP1, with LMP1 stimulating the ubiquitination of RIP and its interaction with IRF7. Moreover, LMP1 stimulates RIP-dependent K63-linked ubiquitination of IRF7, which regulates protein function rather than proteasomal degradation of proteins. We suggest that RIP may serve as a general activator of IRF7, responding to and transmitting the signals from various stimuli, and that ubiquitination may be a general mechanism for enhancing the activity of IRF7.
机译：作为I型干扰素（IFN）（IFN-α/β）反应的关键介质，IFN调节因子7（IRF7）对于宿主免疫防御至关重要。 IRF7的激活通常需要病毒诱导的C末端磷酸化，从而导致其核积累和靶基因的激活。在这里，我们使用激活IRF7的爱泼斯坦-巴尔病毒（EBV）癌蛋白LMP1来识别参与IRF7激活的因子。我们首次证明RIP激活IRF7，并且RIP和IRF7在EBV阳性伯基特氏淋巴瘤细胞的生理条件下相互作用。我们提供的证据表明RIP和IRF7在这些细胞中都是泛素化的，并且IRF7优先与泛素化的RIP相互作用。 RMP是LMP1完全激活IRF7所必需的，而LMP1会刺激RIP的泛素化及其与IRF7的相互作用。此外，LMP1刺激IRF7的依赖RIP的K63连锁泛素化，IRF7调节蛋白质功能而不是蛋白质的蛋白酶体降解。我们建议RIP可以充当IRF7的一般激活剂，响应并传输各种刺激的信号，泛素化可能是增强IRF7活性的一般机制。

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