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

Nature, 2007-04, Vol.446 (7138), p.916-920 [Peer Reviewed Journal]

2007 INIST-CNRS ;COPYRIGHT 2007 Nature Publishing Group ;COPYRIGHT 2007 Nature Publishing Group ;Copyright Nature Publishing Group Apr 19, 2007 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;EISSN: 1476-4679 ;DOI: 10.1038/nature05732 ;PMID: 17392790 ;CODEN: NATUAS

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Title:
TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
Author: Jung, Jae U ; Gack, Michaela U ; Shin, Young C ; Joo, Chul-Hyun ; Urano, Tomohiko ; Liang, Chengyu ; Sun, Lijun ; Takeuchi, Osamu ; Akira, Shizuo ; Chen, Zhijian ; Inoue, Satoshi
Subjects: Amino Acid Motifs ; Biological and medical sciences ; Cell Line ; Cellular biology ; DEAD-box RNA Helicases - chemistry ; DEAD-box RNA Helicases - genetics ; DEAD-box RNA Helicases - metabolism ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Genetics ; Genetics of the immune response ; Humans ; Immunity, Innate ; Immunobiology ; Interferon-beta - biosynthesis ; Interferon-beta - genetics ; Mammals ; NF-kappa B - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Ribonucleic acid ; RNA ; RNA Viruses - immunology ; Signal Transduction ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases - chemistry ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Virology
Is Part Of: Nature, 2007-04, Vol.446 (7138), p.916-920
Description: Retinoic-acid-inducible gene-I (RIG-I; also called DDX58) is a cytosolic viral RNA receptor that interacts with MAVS (also called VISA, IPS-1 or Cardif) to induce type I interferon-mediated host protective innate immunity against viral infection. Furthermore, members of the tripartite motif (TRIM) protein family, which contain a cluster of a RING-finger domain, a B box/coiled-coil domain and a SPRY domain, are involved in various cellular processes, including cell proliferation and antiviral activity. Here we report that the amino-terminal caspase recruitment domains (CARDs) of RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. The carboxy-terminal SPRY domain of TRIM25 interacts with the N-terminal CARDs of RIG-I; this interaction effectively delivers the Lys 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, resulting in a marked increase in RIG-I downstream signalling activity. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction. Furthermore, gene targeting demonstrates that TRIM25 is essential not only for RIG-I ubiquitination but also for RIG-I-mediated interferon- production and antiviral activity in response to RNA virus infection. Thus, we demonstrate that TRIM25 E3 ubiquitin ligase induces the Lys 63-linked ubiquitination of RIG-I, which is crucial for the cytosolic RIG-I signalling pathway to elicit host antiviral innate immunity.
Publisher: London: Nature Publishing
Language: English
Identifier: ISSN: 0028-0836
EISSN: 1476-4687
EISSN: 1476-4679
DOI: 10.1038/nature05732
PMID: 17392790
CODEN: NATUAS
Source: ProQuest One Psychology
MEDLINE
Alma/SFX Local Collection
ProQuest Central

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

2007 INIST-CNRS ;COPYRIGHT 2007 Nature Publishing Group ;COPYRIGHT 2007 Nature Publishing Group ;Copyright Nature Publishing Group Apr 19, 2007 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;EISSN: 1476-4679 ;DOI: 10.1038/nature05732 ;PMID: 17392790 ;CODEN: NATUAS

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