ArticleBritish journal of pharmacology2020
Ring finger protein 219 regulates inflammatory responses by stabilizing sirtuin 1.
Article in British journal of pharmacology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- E3 Ligases and Deubiquitinases in Controlling High-Mobility Group Box (HMGB) Protein Functions.International journal of molecular sciences · 2026Review
- RNF219 RING Finger Domain Mutants Drive Phase Separation to Encapsulate CCR4-NOT and Promote Cell Proliferation.Cell proliferation · 2026Article
- Review
- Myricanol attenuates sepsis-induced inflammatory responses by nuclear factor erythroid 2-related factor 2 signaling and nuclear factor kappa B/mitogen-activated protein kinase pathway via upregulating Sirtuin 1.Inflammopharmacology · 2024Article
- Activation of Sirtuin-1 by Pinocembrin Treatment Contributes to Reduced Early Brain Injury after Subarachnoid Hemorrhage.Oxidative medicine and cellular longevity · 2022Article
- Ring finger protein 219 regulates inflammatory responses by stabilizing sirtuin 1.British journal of pharmacology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
background and purposeRing finger protein 219 (RNF219), a protein containing the C EXPERIMENTAL APPROACH: Effects of RNF219 on SIRT1 were studied in vitro using RAW264.7 cells and in male BALB/c mice, treated with LPS or IFN-γ. Western blots, RT-PCR, co-immunoprecipitation and ubiquitination assays were used, along with LC-MS/MS analysis. In vivo, survival and serum cytokines and tissue levels of RNF219 and SIRT1 were measured. KEY
resultsBinding of RNF219 to SIRT1 inhibited degradation of SIRT1 by preventing its ubiquitination, thereby prolonging SIRT1-mediated anti-inflammatory signalling. LPS caused RNF219 deacetylation, leading to instability of RNF219 and preventing its association with SIRT1. Accordingly, the acetylation status of RNF219 is a critical determinant in its interaction with SIRT1, affecting the response to inflammatory stimuli. The deacetylase inhibitor trichostatin A, increased acetylation and stability of RNF219 and survival of mice injected with LPS, through the interaction of RNF219 with SIRT1. CONCLUSION AND IMPLICATIONS: RNF219 is involved in a novel mechanism to stabilize SIRT1 protein by protein-protein interaction, leading to the resolution of cellular inflammation. These observations provide new insights into the function of RNF219 in modulation of cellular inflammation, and may aid and encourage the development of new anti-inflammatory drugs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.