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Proc Natl Acad Sci U S A. 2009 May 26;106(21):8653-8. doi: 10.1073/pnas.0900850106. Epub 2009 May 11.

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

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  • 1The Education Ministry Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China.

Abstract

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.

PMID:
19433799
[PubMed - indexed for MEDLINE]
PMCID:
PMC2689030
Free PMC Article
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