ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
2009; National Academy of Sciences; Volume: 106; Issue: 21 Linguagem: Inglês
10.1073/pnas.0900850106
ISSN1091-6490
AutoresWenxiang Sun, Yang Li, Lu Chen, Huihui Chen, Fuping You, Xiang Zhou, Yi Zhou, Zhonghe Zhai, Danying Chen, Zhengfan Jiang,
Tópico(s)Inflammasome and immune disorders
ResumoWe 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.
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