Acetylation in pathogenesis: Revealing emerging mechanisms and therapeutic prospects - 12/10/23
, Ran Liu a, ⁎ Abstract |
Protein acetylation modifications play a central and pivotal role in a myriad of biological processes, spanning cellular metabolism, proliferation, differentiation, apoptosis, and beyond, by effectively reshaping protein structure and function. The metabolic state of cells is intricately connected to epigenetic modifications, which in turn influence chromatin status and gene expression patterns. Notably, pathological alterations in protein acetylation modifications are frequently observed in diseases such as metabolic syndrome, cardiovascular disorders, and cancer. Such abnormalities can result in altered protein properties and loss of function, which are closely associated with developing and progressing related diseases. In recent years, the advancement of precision medicine has highlighted the potential value of protein acetylation in disease diagnosis, treatment, and prevention. This review includes provocative and thought-provoking papers outlining recent breakthroughs in acetylation modifications as they relate to cardiovascular disease, mitochondrial metabolic regulation, liver health, neurological health, obesity, diabetes, and cancer. Additionally, it covers the molecular mechanisms and research challenges in understanding the role of acetylation in disease regulation. By summarizing novel targets and prognostic markers for the treatment of related diseases, we aim to contribute to the field. Furthermore, we discuss current hot topics in acetylation research related to health regulation, including N4-acetylcytidine and liquid-liquid phase separation. The primary objective of this review is to provide insights into the functional diversity and underlying mechanisms by which acetylation regulates proteins in disease contexts.
Le texte complet de cet article est disponible en PDF.Graphical Abstract |
Highlights |
• | Enrichment of Nε-acetylation-specific sites is an early clue to disease development. |
• | Non-histone acetylation also emerges as a key 'enforcer' of altered gene regulation. |
• | Chromatin recruits acetylation effectors, crucial for precise gene expression control. |
• | Exploring the key site acetylation elucidates disease-metabolic causal links. |
Abbreviations : BMAL1 , TNF-α , C/EBPδ , GPS2 , BMP4 , LPL , ABCG1 , HK-2 cells , NAD + , TCA , NMN , NADH , mTORC1 , P53 , NF-κB , GAPDH , OPC , Cdk2 , Cyc E , E2F4 , OL , ANT1/2 , G6PD , PPP , NADPH , SMC cells , PPAR , NRVM cells , β-HB , K-ac , K-bhb , CpyD , PD-L1 , RANBP2 , FTO , m6A , GNAO1 , HP1γ , MDC1 , NAT10 , KIF23 , ac4C , FSP1 , H pylori , AGS cells , MDM2 , 3'UTR , IDR1 , DDX3X , LLPS , YY1 , METTL3
Keywords : Protein acetylation, Epigenetic modifications, Precision medicine, Molecular mechanism, Therapeutic targets
Plan
Vol 167
Article 115519- novembre 2023 Retour au numéro
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