| Autor: |
Hong-Xin Zhang, Zi-Xing Liu, Yue-Ping Sun, Jiang Zhu, Shun-Yuan Lu, Xue-Song Liu, Qiu-Hua Huang, Yin-Yin Xie, Hou-Bao Zhu, Su-Ying Dang, Hai-Feng Chen, Guang-Yong Zheng, Yi-Xue Li, Ying Kuang, Jian Fei, Sai-Juan Chen, Zhu Chen, Zhu-Gang Wang |
| Předmět: |
|
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; 4/16/2013, Vol. 110 Issue 16, p6459-6464, 6p |
| Abstrakt: |
Retinoic acid inducible gene I (RIG-I) senses viral RNA5 and triggers innate antiviral responses through induction of type I IFN5 and inflammatory cytokines. However, whether RIG-I interacts with host cellular RNA remains undetermined. Here we report that Rig-I interacts with multiple cellular mRNAs, especially Nf-κBl. Rig-I is required for NF-κBactivity via regulating F4f-icbl expression at posttranscriptional levels. It interacts with the multiple binding sites within 3'-UTR of Nf-icbl mRNA. Further analyses reveal that three distinct tandem motifs enriched in the 3'-UTR fragments can be recognized by Rig-I. The 3'-UTR binding with Rig-I plays a critical role in normal translation of Nf-κBl by recruiting the ribosomal proteins [ribosomal protein L13 (Rp113) and Rpl8~ and rRNAS (18S and 285). Down-regulation of Rig-I or Rpll3 significantly reduces Nf-icbl and 3'-UTR-mediated luciferase expression levels. These findings indicate that Rig-I functions as a positive regulator for NF-κBsignaling and is involved in multiple biological processes in addition to host antivirus immunity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
