ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
TRIM38 Suppresses Breast Cancer Progression via Modulating SQSTM1 Ubiquitination and Autophagic Flux.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 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
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
2 citing papers in PubMed.
- Review
- The oncogenic signalosome: SQSTM1/p62 as a master integrator of signaling, metabolism, and autophagy in cancer.Toxicological research · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors.
Funding
Abstract
TRIM38, an E3 ubiquitin-protein ligase, has previously been implicated in innate immune and inflammatory responses, yet its role in breast cancer regulation remains unclear. This study elucidates the suppressive function of TRIM38 in breast cancer progression. The results indicate a decreased expression of TRIM38 in breast cancer tissues compared to adjacent non-cancerous counterparts, and its reduced expression correlates with unfavorable clinical outcomes in breast cancer patients. Both in vitro and in vivo experiments demonstrate that TRIM38 inhibits breast cancer proliferation, migration, and invasion. Furthermore, an inverse regulatory relationship between TRIM38 protein level and autophagic flux is observed. Mechanistically, SQSTM1/p62 is identified as a novel substrate of TRIM38, which promotes non-degradative K63-linked ubiquitination at SQSTM1 K420 residue. This kind of ubiquitination disrupts the interaction between SQSTM1 and LC3, thereby impeding autophagic flux. Collectively, the findings underscore TRIM38 as a crucial regulator of autophagy and present novel, promising therapeutic targets for breast cancer.
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.