ZNFX1 uses two-component ubiquitin circuitry to quarantine viral RNA

Daniel R. Squair^1,‡, Eilidh Rivers^2,‡, Hanna Sowar², Arda Balci², Roosa Harmo², David J. Wright¹, Gaurav Beniwal¹, Mathieu Soetens¹, Sunil Mathur¹, Aidan Tollervey², Nicola T. Wood¹, Kuan-Chuan Pao¹, Callum Stanton¹, Adam J. Fletcher^2,* and Satpal Virdee^1,*

Molecular Cell

Highlights

Activity-based E3 ligase profiling identifies ZNFX1 as an atypical E3 ligase
ATP-dependent RNA binding to the SF1 helicase domain activates dual E3 ligase function
E3 activity and ATP-dependent RNA binding are required for broad viral restriction
ZNFX1 drives ubiquitin-regulated RNA sequestration into self-propagating aggregates

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