1. Academic Validation
  2. ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization

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

  • Proc Natl Acad Sci U S A. 2009 May 26;106(21):8653-8. doi: 10.1073/pnas.0900850106.
Wenxiang Sun 1 Yang Li Lu Chen Huihui Chen Fuping You Xiang Zhou Yi Zhou Zhonghe Zhai Danying Chen Zhengfan Jiang
Affiliations

Affiliation

  • 1 The 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.

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