ArticleInternational journal of clinical oncology2026
RNF125 mediates the anti-breast cancer activity of betulinic acid through ubiquitin-dependent degradation of MYH9.
Article in International journal of clinical oncology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
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
backgroundBreast cancer (BC) represents one of the leading causes of cancer-related mortality in women worldwide. Betulinic acid (BA), a naturally derived pentacyclic triterpenoid, exhibits anti-BC activity. Recent evidence implicates RNF125, a RING-domain E3 ubiquitin ligase, as a tumor suppressor. This study aimed to elucidate whether BA exerts anti-BC effects via RNF125 regulation and explored the underlying mechanisms.
methodsRNF125-overexpressing or knockdown BC cell lines were generated to examine the regulatory effect on cell proliferation, motility, and invasiveness. Furthermore, a subcutaneous xenograft mouse model was established to evaluate the influence of RNF125 on tumor growth in vivo.
resultsBioinformatics analyses revealed BA-mediated upregulation of RNF125 in BC cells. Pan-cancer data indicated reduced RNF125 expression in BC specimens, correlating with unfavorable survival outcomes. Consistently, our results showed that BA upregulates RNF125 protein expression in a concentration-dependent manner. In clinically collected BC samples, diminished RNF125 expression was significantly associated with advanced TNM staging. Functional assays demonstrated that RNF125 overexpression suppressed cell proliferation, migration, and invasion. Conversely, RNF125 knockdown reversed these effects and abrogated BA-mediated suppression of malignant phenotypes in BC cells. Mechanistically, RNF125 interacted with MYH9 (Myosin Heavy Chain 9) to facilitate its ubiquitin-mediated proteasomal degradation. In BA-treated BC cells, the protein expression of MYH9 was inhibited. Ectopic MYH9 expression reversed the tumor-suppressive effects of RNF125 overexpression. Finally, a murine xenograft model confirmed that RNF125 overexpression inhibits BC tumor growth.
conclusionThese findings suggested that RNF125 mediates the anti-tumor effect of BA, at least in part, through ubiquitin-dependent degradation of MYH9.
Indexed as
Identifiers
42315734What Socratic 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 Socratic graph.