ArticleJournal of translational medicine2025
Acetylation suppresses breast cancer progression by sustaining CLYBL stability.
Article in Journal of translational medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Advances in Mechanism of Action and Efficacy of CBP/p300 Inhibitors in Different Subtypes of Breast Cancer.Molecules (Basel, Switzerland) · 2026Review
- The role of KPNA3 in multiple myeloma: implications for targeting nuclear import.Apoptosis : an international journal on programmed cell death · 2026Article
- Comprehensive characterization of the molecular feature of acetylation in colorectal cancer using integrated single-cell and bulk RNA sequencing.Scientific reports · 2025Article
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Authors and funding
14 authors.
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Abstract
backgroundThe incidence of breast cancer remains high and it remains the leading cause of cancer-related deaths in women. A better understanding of the molecular mechanisms of breast cancer and identifying novel biomarkers will help improve therapeutic strategies. Citrate lyase beta like (CLYBL) is expressed at low levels in breast cancer tissues and is associated with low patient survival rates. In this study, we explored the regulatory mechanisms of CLYBL and its acetylation in breast cancer.
methodsCLYBL expression patterns in breast cancer were assessed using a breast cancer tissue microarray, immunohistochemistry, and publicly available datasets. The acetylation patterns of CLYBL and the related regulatory functions were detected by high resolution mass spectrometry, immunoprecipitation assays, and western blot analysis. The potential effects of CLYBL and its acetylation on breast cancer were determined using both in vitro and in vivo assays.
resultsCLYBL was expressed at lower levels in breast cancer samples compared with normal tissues. This low CLYBL expression was associated with poor patient survival rates. Overexpressing CLYBL could inhibit breast cancer and reduce NRF2 pathway-mediated antioxidants. We identified two acetylated lysine sites in CLYBL, K57 and K82, using acetylated peptide affinity enrichment and high-resolution mass spectrometry. Our results suggest that K82 is the main acetylation site. Further work showed that the p300/CBP associated factor (PCAF) and histone deacetylase 3 (HDAC3) as the CLYBL acetyltransferase and deacetylase, respectively. Additionally, CLYBL acetylation facilitates its own protein stability by reducing it affinity for ubiquitin, thus enhancing the anti-breast cancer effects.
conclusionWe revealed the role of CLYBL overexpression and its acetylation in breast cancer. Our study suggests that CLYBL is a potential molecular target for breast cancer therapy.
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