Sun Wenxiang, Li Yang, Chen Lu, Chen Huihui, You Fuping, Zhou Xiang, Zhou Yi, Zhai Zhonghe, Chen Danying, Jiang Zhengfan
The Education Ministry Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China.
Proc Natl Acad Sci U S A. 2009 May 26;106(21):8653-8. doi: 10.1073/pnas.0900850106. Epub 2009 May 11.
We report here the identification and characterization of a protein, ERIS, an endoplasmic reticulum (ER) IFN stimulator, which is a strong type I IFN stimulator and plays a pivotal role in response to both non-self-cytosolic RNA and dsDNA. ERIS (also known as STING or MITA) resided exclusively on ER membrane. The ER retention/retrieval sequence RIR was found to be critical to retain the protein on ER membrane and to maintain its integrity. ERIS was dimerized on innate immune challenges. Coumermycin-induced ERIS dimerization led to strong and fast IFN induction, suggesting that dimerization of ERIS was critical for self-activation and subsequent downstream signaling.
我们在此报告一种蛋白质ERIS的鉴定与特性，它是一种内质网（ER）干扰素刺激因子，是一种强大的I型干扰素刺激因子，在对非自身胞质RNA和双链DNA的应答中起关键作用。ERIS（也称为STING或MITA）仅存在于内质网膜上。内质网保留/回收序列RIR被发现对于将该蛋白质保留在内质网膜上并维持其完整性至关重要。在先天免疫刺激下，ERIS会发生二聚化。香豆霉素诱导的ERIS二聚化导致强烈且快速的干扰素诱导，这表明ERIS的二聚化对于自我激活及随后的下游信号传导至关重要。
