ArticleCell proliferation2026
RNF219 RING Finger Domain Mutants Drive Phase Separation to Encapsulate CCR4-NOT and Promote Cell Proliferation.
Article in Cell proliferation, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- NEDAMSS syndrome-related truncating and missense mutations are associated with aberrant liquid-liquid phase separation of IRF2BPL.Nature communications · 2026Article
- RNF219 RING Finger Domain Mutants Drive Phase Separation to Encapsulate CCR4-NOT and Promote Cell Proliferation.Cell proliferation · 2026Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
RING finger protein 219 (RNF219) is a co-factor for the CCR4-NOT deadenylase complex in mammals. Here, we found that mutations within the C3HC4 scaffold of the RING finger domain in RNF219 are capable of forming condensates via liquid-liquid phase separation (LLPS), though the wild-type RING finger domain intrinsically suppresses LLPS. We further demonstrated that the adjacent coiled-coil 1 (CC1) domain promotes the potential of RNF219 to form condensates. Moreover, the mutant RNF219 condensates are able to encapsulate the CCR4-NOT complex, inhibiting the RNA deadenylation activity of CCR4-NOT. Additionally, we observed that RNF219 mutations could promote cell proliferation. These findings suggest a pathogenic mechanism whereby RNF219 mutations could induce CCR4-NOT condensate formation, inhibit deadenylation-dependent mRNA decay and drive cell proliferation.
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Registered trials
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