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J Immunol. 2010 Jun 1;184(11):6249-55. doi: 10.4049/jimmunol.0903748. Epub 2010 May 5.

The E3 ubiquitin ligase RNF5 targets virus-induced signaling adaptor for ubiquitination and degradation.

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1
College of Life Sciences, Wuhan University, Wuhan, China.

Abstract

Viral infection activates transcription factors, such as NF-kappaB and IFN regulatory factor 3, which collaborate to induce type I IFNs and elicit innate antiviral response. Virus-induced signaling adaptor (VISA) has been identified as a critical adaptor required for virus-triggered induction of type I IFNs. In this study, we showed that the E3 ubiquitin ligase RING-finger protein 5 (RNF5) interacted with VISA at mitochondria in a viral infection-dependent manner. Domain mapping experiments indicated that the C-terminal transmembrane domain of VISA was required for its interaction with RNF5. RNF5 targeted VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection, whereas knockdown of RNF5 reversed virus-induced downregulation of VISA at the early phase. These findings suggest that RNF5-mediated ubiquitination and degradation of VISA is one of the mechanisms of the regulation of virus-triggered induction of type I IFNs and cellular antiviral response.

PMID:
20483786
DOI:
10.4049/jimmunol.0903748
[Indexed for MEDLINE]
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