ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization | Zendy

Wenxiang Sun | Zendy; Yang Li | Zendy; Lu Chen | Zendy; Huihui Chen | Zendy; Fuping You | Zendy; Xiang Zhou | Zendy; Yi Zhou | Zendy; Zhonghe Zhai | Zendy; Danying Chen | Zendy; Zhengfan Jiang | Zendy

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ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization

Author(s) -

Wenxiang Sun,

Yang Li,

Lu Chen,

Huihui Chen,

Fuping You,

Xiang Zhou,

Yi Zhou,

Zhonghe Zhai,

Danying Chen,

Zhengfan Jiang

Publication year - 2009

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.0900850106

Subject(s) - endoplasmic reticulum , stimulator of interferon genes , innate immune system , microbiology and biotechnology , signal transduction , biology , er retention , stim1 , interferon , cytosol , immune system , immunology , gene , biochemistry , mutant , enzyme

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.

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