Stimulator of interferon genes (STING) plays important roles in the DNA-mediated innate immune responses. However, the regulatory mechanism of STING in terms of stabilization is not fully understood. Here, we identified the chaperone protein Hsp90s as novel STING interacting proteins. Treatment with an Hsp90 inhibitor 17-AAG and knockdown of Hsp90β but not Hsp90α reduced STING at protein level, resulted in the suppression of IFN induction in response to stimulation with cGAMP, and infections with HSV-1 and Listeria monocytogenes. Collectively, our results suggest that the control of STING protein by Hsp90β is a critical biological process in the DNA sensing pathways.

干扰素基因的刺激物（STING）在DNA介导的先天免疫反应中起重要作用。但是，关于稳定性的STING调节机制尚不完全清楚。在这里，我们确定了伴侣蛋白Hsp90s为新型STING相互作用蛋白。用Hsp90抑制剂17-AAG处理并敲除Hsp90β而不是Hsp90α可以降低蛋白水平的STING，导致对cGAMP刺激产生的IFN诱导抑制作用以及HSV-1和单核细胞增生李斯特菌感染。总体而言，我们的结果表明，Hsp90β对STING蛋白的控制是DNA传感途径中的关键生物学过程。