Split-site ubiquitination gives ZNFX1 new power in RNA defense.
Publication
, Journal Article
Horner, SM
Published in: Mol Cell
October 16, 2025
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.
Duke Scholars
Published In
Mol Cell
DOI
EISSN
1097-4164
Publication Date
October 16, 2025
Volume
85
Issue
20
Start / End Page
3734 / 3736
Location
United States
Related Subject Headings
- Ubiquitination
- Ubiquitin-Protein Ligases
- Ubiquitin
- RNA
- Protein Domains
- Lysine
- Humans
- Developmental Biology
- Animals
- 42 Health sciences
Citation
APA
Chicago
ICMJE
MLA
NLM
Horner, S. M. (2025). Split-site ubiquitination gives ZNFX1 new power in RNA defense. Mol Cell, 85(20), 3734–3736. https://doi.org/10.1016/j.molcel.2025.09.022
Horner, Stacy M. “Split-site ubiquitination gives ZNFX1 new power in RNA defense.” Mol Cell 85, no. 20 (October 16, 2025): 3734–36. https://doi.org/10.1016/j.molcel.2025.09.022.
Horner SM. Split-site ubiquitination gives ZNFX1 new power in RNA defense. Mol Cell. 2025 Oct 16;85(20):3734–6.
Horner, Stacy M. “Split-site ubiquitination gives ZNFX1 new power in RNA defense.” Mol Cell, vol. 85, no. 20, Oct. 2025, pp. 3734–36. Pubmed, doi:10.1016/j.molcel.2025.09.022.
Horner SM. Split-site ubiquitination gives ZNFX1 new power in RNA defense. Mol Cell. 2025 Oct 16;85(20):3734–3736.
Published In
Mol Cell
DOI
EISSN
1097-4164
Publication Date
October 16, 2025
Volume
85
Issue
20
Start / End Page
3734 / 3736
Location
United States
Related Subject Headings
- Ubiquitination
- Ubiquitin-Protein Ligases
- Ubiquitin
- RNA
- Protein Domains
- Lysine
- Humans
- Developmental Biology
- Animals
- 42 Health sciences