TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity

Michaela U. Gack, Young C. Shin, Chul-Hyun Joo, Tomohiko Urano, Chengyu Liang, Lijun Sun, Osamu Takeuchi, Shizuo Akira, Zhijian Chen, Satoshi Inoue and Jae U. Jung ()
Additional contact information
Michaela U. Gack: New England Primate Research Center, Harvard Medical School, 1 Pine Hill Drive, Southborough, Massachusetts 01772, USA
Young C. Shin: New England Primate Research Center, Harvard Medical School, 1 Pine Hill Drive, Southborough, Massachusetts 01772, USA
Chul-Hyun Joo: New England Primate Research Center, Harvard Medical School, 1 Pine Hill Drive, Southborough, Massachusetts 01772, USA
Tomohiko Urano: Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-8655, Japan
Chengyu Liang: New England Primate Research Center, Harvard Medical School, 1 Pine Hill Drive, Southborough, Massachusetts 01772, USA
Lijun Sun: University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148, USA
Osamu Takeuchi: Japan Science and Technology Agency, Osaka 565-0871, Japan
Shizuo Akira: Japan Science and Technology Agency, Osaka 565-0871, Japan
Zhijian Chen: University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148, USA
Satoshi Inoue: Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-8655, Japan
Jae U. Jung: New England Primate Research Center, Harvard Medical School, 1 Pine Hill Drive, Southborough, Massachusetts 01772, USA

Nature, 2007, vol. 446, issue 7138, 916-920

Abstract: The cytoplasmic receptor RIG-I recognizes viral RNAs and initiates a protective innate immune response against a number of important viruses. Here, it is shown that RIG-I is regulated by ubiquitination.

Date: 2007
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DOI: 10.1038/nature05732

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