ArticleCell death & disease2025
Acetylation-dependent USP7-TRIM25 axis drives oncogenic progression in non-small cell lung cancer.
Article in Cell death & disease, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- KRAS/ERK2-driven stabilization of AARS1 reprograms tumor metabolism and confers Sorafenib resistance in lung adenocarcinoma.Cell death and differentiation · 2026Article
- SIRT5-dependent desuccinylation licenses UBR5-mediated degradation of TAMM41 to regulate mitochondrial metabolism in lung adenocarcinoma.Biology direct · 2026Article
- Elevated TRIM25 Impairs Poly (ADP-ribose) Metabolism via PARG Degradation and Mediates Compression-Induced Intervertebral Disc Degeneration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Yifei Sanjie Formula in improving the response to PD-1 blockade by lung cancer through the attenuation of the USP7-NR1H4-bile acid metabolism axis.Journal of thoracic disease · 2026Article
- The role of TRIM proteins in the pathogenesis of mycobacterium tuberculosis.Biology direct · 2025Review
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Authors and funding
16 authors.
Funding
Abstract
Tripartite motif containing 25 (TRIM25), an E3 ubiquitin ligase that plays an important role in bioprocesses, is frequently elevated in malignant tumors. However, it remains unclear how TRIM25 protein expression is regulated in non-small cell lung cancer (NSCLC). Here, we find that TRIM25 is hyper-expressed in NSCLC tissues and associated with poor prognosis of NSCLC patients. Both in vitro and in vivo experiments indicate that TRIM25 facilitates tumor proliferation and metastasis. Mechanistically, acetylation is identified as a critical post-translational modification (PTM) regulating TRIM25 protein stability in NSCLC. The lysine acetyltransferase cAMP-responsive element-binding (CREB)-binding protein (CBP) mediates acetylation of TRIM25 at lysine 392, which is counteracted by the deacetylase Sirtuin 7 (SIRT7). Notably, the acetylation of TRIM25 enhances its interaction with ubiquitin specific peptidase 7 (USP7), resulting in reduced ubiquitination of TRIM25. In summary, our study reveals a novel acetylation modification site, thus providing new insights into an epigenetic regulation of TRIM25 in human cancer, and suggesting that pharmacological inhibition of TRIM25 acetylation is a potential anti-tumor strategy.
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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.