Faculty of Pharmacy, Université de Montréal, Montréal, Québec Canada.
PLoS Pathog. 2012;8(7):e1002747. doi: 10.1371/journal.ppat.1002747. Epub 2012 Jul 5.
Tumor Necrosis Factor receptor-associated factor-3 (TRAF3) is a central mediator important for inducing type I interferon (IFN) production in response to intracellular double-stranded RNA (dsRNA). Here, we report the identification of Sec16A and p115, two proteins of the ER-to-Golgi vesicular transport system, as novel components of the TRAF3 interactome network. Notably, in non-infected cells, TRAF3 was found associated with markers of the ER-Exit-Sites (ERES), ER-to-Golgi intermediate compartment (ERGIC) and the cis-Golgi apparatus. Upon dsRNA and dsDNA sensing however, the Golgi apparatus fragmented into cytoplasmic punctated structures containing TRAF3 allowing its colocalization and interaction with Mitochondrial AntiViral Signaling (MAVS), the essential mitochondria-bound RIG-I-like Helicase (RLH) adaptor. In contrast, retention of TRAF3 at the ER-to-Golgi vesicular transport system blunted the ability of TRAF3 to interact with MAVS upon viral infection and consequently decreased type I IFN response. Moreover, depletion of Sec16A and p115 led to a drastic disorganization of the Golgi paralleled by the relocalization of TRAF3, which under these conditions was unable to associate with MAVS. Consequently, upon dsRNA and dsDNA sensing, ablation of Sec16A and p115 was found to inhibit IRF3 activation and anti-viral gene expression. Reciprocally, mild overexpression of Sec16A or p115 in Hec1B cells increased the activation of IFNβ, ISG56 and NF-κB -dependent promoters following viral infection and ectopic expression of MAVS and Tank-binding kinase-1 (TBK1). In line with these results, TRAF3 was found enriched in immunocomplexes composed of p115, Sec16A and TBK1 upon infection. Hence, we propose a model where dsDNA and dsRNA sensing induces the formation of membrane-bound compartments originating from the Golgi, which mediate the dynamic association of TRAF3 with MAVS leading to an optimal induction of innate immune responses.
肿瘤坏死因子受体相关因子 3(TRAF3)是一种重要的中介因子,可诱导细胞内双链 RNA(dsRNA)产生 I 型干扰素(IFN)。在这里,我们报告了 Sec16A 和 p115 的鉴定,这两种内质网到高尔基体囊泡运输系统的蛋白质是 TRAF3 相互作用网络的新成员。值得注意的是,在未感染的细胞中,TRAF3 与内质网出口位点(ERES)、内质网到高尔基体中间区(ERGIC)和顺面高尔基器的标志物相关联。然而,在 dsRNA 和 dsDNA 感应后,高尔基器碎裂成含有 TRAF3 的细胞质点状结构,允许其共定位和与线粒体抗病毒信号(MAVS)相互作用,MAVS 是必需的线粒体结合 RIG-I 样解旋酶(RLH)衔接蛋白。相比之下,TRAF3 在 ER 到高尔基体囊泡运输系统中的保留,削弱了 TRAF3 在病毒感染时与 MAVS 相互作用的能力,从而降低了 I 型 IFN 反应。此外,Sec16A 和 p115 的耗竭导致高尔基器的严重紊乱,同时 TRAF3 重新定位,在这些条件下,TRAF3 无法与 MAVS 相关联。因此,在 dsRNA 和 dsDNA 感应后,Sec16A 和 p115 的缺失被发现抑制了 IRF3 的激活和抗病毒基因的表达。相反,在 Hec1B 细胞中轻度过表达 Sec16A 或 p115,可增加病毒感染和异位表达 MAVS 和 Tank-binding kinase-1(TBK1)后 IFNβ、ISG56 和 NF-κB 依赖性启动子的激活。与这些结果一致,在感染后,TRAF3 被发现富集在由 p115、Sec16A 和 TBK1 组成的免疫复合物中。因此,我们提出了一个模型,即 dsDNA 和 dsRNA 感应诱导源自高尔基体的膜结合区室的形成,该区室介导 TRAF3 与 MAVS 的动态关联,从而最佳地诱导先天免疫反应。