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Updated: Jan 14, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
Published on: May 10, 2022
Split-site ubiquitination gives ZNFX1 new power in RNA defense
1Department of Integrative Immunobiology, Duke University School of Medicine, Durham, NC, USA; Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, NC, USA; Department of Medicine, Duke University School of Medicine, Durham, NC, USA.
Abstract:
Recent work by Grabarczyk et al.1 uncovers the molecular mechanism by which ZNFX1, an interferon-stimulated gene, employs a novel split-site E3 ligase domain structure to ubiquitinate both protein lysine residues and RNA 2' hydroxyls. This activity enables ZNFX1 to compact pathogenic RNA into dense, ubiquitin-coated particles, revealing a new modality for interferon-induced antiviral defense.
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