RGD Reference Report - Cyclophilin A-regulated ubiquitination is critical for RIG-I-mediated antiviral immune responses. - Rat Genome Database

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Cyclophilin A-regulated ubiquitination is critical for RIG-I-mediated antiviral immune responses.

Authors: Liu, Wei  Li, Jing  Zheng, Weinan  Shang, Yingli  Zhao, Zhendong  Wang, Shanshan  Bi, Yuhai  Zhang, Shuang  Xu, Chongfeng  Duan, Ziyuan  Zhang, Lianfeng  Wang, Yue L  Jiang, Zhengfan  Liu, Wenjun  Sun, Lei 
Citation: Liu W, etal., Elife. 2017 Jun 8;6. doi: 10.7554/eLife.24425.
RGD ID: 150429629
Pubmed: (View Article at PubMed) PMID:28594325
DOI: Full-text: DOI:10.7554/eLife.24425

RIG-I is a key cytosolic pattern recognition receptor that interacts with MAVS to induce type I interferons (IFNs) against RNA virus infection. In this study, we found that cyclophilin A (CypA), a peptidyl-prolyl cis/trans isomerase, functioned as a critical positive regulator of RIG-I-mediated antiviral immune responses. Deficiency of CypA impaired RIG-I-mediated type I IFN production and promoted viral replication in human cells and mice. Upon Sendai virus infection, CypA increased the interaction between RIG-I and its E3 ubiquitin ligase TRIM25, leading to enhanced TRIM25-mediated K63-linked ubiquitination of RIG-I that facilitated recruitment of RIG-I to MAVS. In addition, CypA and TRIM25 competitively interacted with MAVS, thereby inhibiting TRIM25-induced K48-linked ubiquitination of MAVS. Taken together, our findings reveal an essential role of CypA in boosting RIG-I-mediated antiviral immune responses by controlling the ubiquitination of RIG-I and MAVS.



Disease Annotations    

Objects Annotated

Genes (Rattus norvegicus)
Ppia  (peptidylprolyl isomerase A)

Genes (Mus musculus)
Ppia  (peptidylprolyl isomerase A)

Genes (Homo sapiens)
PPIA  (peptidylprolyl isomerase A)


Additional Information