ArticleOncogene2026
YME1L1 degradation by TRIM21 inhibits bladder cancer proliferation, metastasis, and mitochondrial function.
Article in Oncogene, 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
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bladder cancer is a common and aggressive disease with limited treatment options, highlighting the urgent need for new therapeutic strategies. Although mitochondrial proteins have been implicated in cancer progression, their role in bladder cancer remains unclear. This study aimed to investigate the function of the mitochondrial protease YME1L1 and its regulation by the E3 ubiquitin ligase TRIM21. By analyzing patient tissue samples, single-cell RNA data and performing experiments manipulating YME1L1 and TRIM21 levels in bladder cancer cells, we found that YME1L1 promotes cancer cell proliferation, invasion and mitochondrial energy production. Mechanistically, TRIM21 interacts with YME1L1 through its SPRY domain, facilitating K63-linked polyubiquitination of YME1L1 and accelerating its degradation. Furthermore, the K237 residue of YME1L1 is critical for TRIM21-mediated ubiquitination. These findings suggest that targeting the TRIM21-YME1L1 pathway could offer a novel strategy to inhibit bladder cancer progression.
Indexed as
Identifiers
42477459What 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.