Calpain 15 activity in immune regulation

先天免疫系统由传感器和信号分子网络组成。这一系统的调节非常复杂，而且只有部分了解。然而，所有传播的病毒都进化到扰乱这个系统，以传播它们的传播。我们使用亲和蛋白质组学方法来鉴定先天免疫系统中迄今未知的成分。通过这些筛选，我们确定了蛋白酶钙蛋白酶15（CAPN 15）作为Thogotovirus的免疫调节蛋白ML的相互作用伴侣。初步实验表明，CAPN 15与TRAF 2和DIABLO相互作用，TRAF 2和DIABLO是TNF依赖性NF-kB信号通路的组分。CAPN 15在功能上调节TNF依赖性信号传导，但不影响IL 1-β引起的信号传导。在这里，我们建议研究CAPN 15对先天免疫系统的功能。我们计划使用功能和蛋白质组学分析的组合，并在体内研究CAPN 15的功能。

The innate immune system consists of a network of sensors and signalling molecules. The regulation of this system is very complex and only partially understood. However, all circulating viruses evolutionary evolved to perturb this system in order to propagate their spread. We used an affinity proteomics approach to identify hitherto unknown components of the innate immune system. Through these screens we identified the protease calpain 15 (CAPN15) as interaction partner of the immunomodulatory protein ML of Thogotovirus. Preliminary experiments show that CAPN15 interacts with TRAF2 and DIABLO, which are components of the TNF-dependent NF-kB signaling pathway. Functionally CAPN15 regulates TNF-dependent signaling, but does not influence signaling elicited by IL1-beta. Here we propose to study the function of CAPN15 for the innate immune system. We plan to use a combination of functional and proteomic analyses and to study the function of CAPN15 in vivo.