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

Bo Zhong, Yu Zhang, Bo Tan, Tian Tian Liu, Yan Yi Wang, Hong Bing Shu

Research output: Contribution to journalArticlepeer-review

150 Scopus citations

Abstract

Viral infection activates transcription factors, such as NF-κB 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 down-regulation 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.

Original languageEnglish
Pages (from-to)6249-6255
Number of pages7
JournalJournal of Immunology
Volume184
Issue number11
DOIs
StatePublished - Jun 1 2010

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