Key result
Ubiquitination regulates AF pathogenesis by modulating inflammation, calcium dysregulation, ferroptosis, oxidative stress, and autophagy.
Why the study?
AF remains a leading cause of cardiovascular morbidity and mortality, while emerging evidence implicates ubiquitination as a central regulator of its pathogenesis.
Ubiquitin-related enzymes play multifaceted roles in atrial fibrillation pathogenesis, highlighting the ubiquitin-proteasome system as a potential therapeutic target.
Identifies ubiquitin-proteasome system as potential AF therapeutic target; extends pathogenic insights and leaves open clinical translation.
Atrial fibrillation (AF) is the most prevalent cardiac arrhythmia, defined by rapid and irregular atrial activation. Despite advances in AF treatment, AF remains a leading cause of cardiovascular morbidity and mortality worldwide. Emerging evidence demonstrates that ubiquitination, a dynamic post-translational modification, acts as a central regulator of AF pathogenesis by modulating inflammatory signaling, calcium dysregulation, ferroptosis, oxidative stress, and autophagy. This review systematically explores the multifaceted roles of ubiquitin-related enzymes (E3 ligases and deubiquitinating enzymes, DUBs) in AF pathogenesis, with an emphasis on their interactions with core molecular pathways. Furthermore, we discuss potential therapeutic strategies targeting the ubiquitin-proteasome system, and provide a framework for future translational research in AF.
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Runtian et al. (2026) conducted a review in Atrial fibrillation. Ubiquitination acts as a central regulator of atrial fibrillation pathogenesis by modulating inflammatory signaling, calcium dysregulation, ferroptosis, oxidative stress, and autophagy.
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