ArticleKidney international2025
UBC9-associated SUMOylation contributes to β-catenin activation and kidney fibrosis.
Article in Kidney international, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
3 citing papers in PubMed.
- UBC9-mediated p53 SUMOylation drives tubular senescence and exacerbates acute kidney injury in mice.Acta pharmacologica Sinica · 2026Article
- Post‑translational modifications in diabetic kidney disease (Review).International journal of molecular medicine · 2026Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
Abstract
introductionSUMOylation is a form of post-translational modification that conjugates a small ubiquitin-like modifier (SUMO) to specific lysine residues of target proteins. The role and regulation of SUMOylation in kidney physiology and pathogenesis are largely unknown. Here, we report that SUMOylation promotes kidney fibrosis by enhancing β-catenin signaling.
methodsUBC9, the sole E2 conjugating enzyme in SUMOylation, was ablated from proximal tubules to determine the role of SUMOylation in mouse kidney fibrosis after obstructed nephropathy or ischemia-reperfusion injury. Point mutations were introduced to identify the SUMOylation sites in β-catenin.
resultsUBC9 was induced in tissues from patients with obstructive or IgA nephropathies and in mouse fibrotic kidneys. Kidney fibrosis in mouse models was alleviated by pharmacological inhibitors of SUMOylation or by UBC9 knockout from kidney proximal tubules. Consistently, knockdown of UBC9 attenuated transforming growth factor-β-induced fibrotic changes in kidney tubular cells in vitro. Mechanistically, fibrotic stress increased the SUMOylation of β-catenin, which contributed to the stability and activation of β-catenin. We further identified three SUMOylation sites in β-catenin, the mutation of which reduced the stability and activation of β-catenin during fibrotic stress.
conclusionsOur results unveil a novel role of SUMOylation in kidney fibrogenesis by activating β-catenin, suggesting a new anti-fibrosis strategy.
Indexed as
Identifiers
What OpenQuestion holds
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.