ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization.
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.
The Education Ministry Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China.
Wenxiang
W
Sun
Yang
Y
Li
Lu
L
Chen
Huihui
H
Chen
Fuping
F
You
Xiang
X
Zhou
Yi
Y
Zhou
Zhonghe
Z
Zhai
Danying
D
Chen
Zhengfan
Z
Jiang
D000818:Animals; D002460:Cell Line; D004721:Endoplasmic Reticulum / Q000276:immunology / Q000378:metabolism; D006801:Humans; D007113:Immunity, Innate / Q000276:immunology*; D008565:Membrane Proteins / Q000276:immunology* / Q000378:metabolism; D051379:Mice; D055503:Protein Multimerization / Q000276:immunology*; D015398:Signal Transduction / Q000276:immunology*; D015854:Up-Regulation / Q000276:immunology
C523851:CISD2 protein, human; D008565:Membrane Proteins