ArticleThe Journal of cell biology2022
GCN5 maintains muscle integrity by acetylating YY1 to promote dystrophin expression.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Early-Life Manganese Overexposure Activates Microglial Phagocytosis through the YY1/TREM2 Axis Leading to Hippocampal Synaptic Remodeling in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The Functions and Regulatory Mechanisms of Histone Modifications in Skeletal Muscle Development and Disease.International journal of molecular sciences · 2025Review
- Epigenetics of Skeletal Muscle Atrophy.International journal of molecular sciences · 2024Review
- Deletion of TECRL promotes skeletal muscle repair by up-regulating EGR2.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Oral administration of ginseng berry concentrate improves lactate metabolism and increases endurance performance in mice.BMB reports · 2023Article
- The Males Absent on the First (MOF) Mediated Acetylation Alters the Protein Stability and Transcriptional Activity of YY1 in HCT116 Cells.International journal of molecular sciences · 2023Article
- The epigenetic regulatory effect of histone acetylation and deacetylation on skeletal muscle metabolism-a review.Frontiers in physiology · 2023Review
- Regulation of alphaherpesvirus protein via post-translational phosphorylation.Veterinary research · 2022Review
- The regulatory network of potential transcription factors and MiRNAs of mitochondria-related genes for sarcopenia.Frontiers in genetics · 2022Article
- Artificial-intelligence-driven discovery of prognostic biomarker for sarcopenia.Journal of cachexia, sarcopenia and muscle · 2021Article
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Authors and funding
14 authors at 6 institutions in 5 countries.
Funding
Abstract
Protein lysine acetylation is a post-translational modification that regulates protein structure and function. It is targeted to proteins by lysine acetyltransferases (KATs) or removed by lysine deacetylases. This work identifies a role for the KAT enzyme general control of amino acid synthesis protein 5 (GCN5; KAT2A) in regulating muscle integrity by inhibiting DNA binding of the transcription factor/repressor Yin Yang 1 (YY1). Here we report that a muscle-specific mouse knockout of GCN5 (Gcn5skm-/-) reduces the expression of key structural muscle proteins, including dystrophin, resulting in myopathy. GCN5 was found to acetylate YY1 at two residues (K392 and K393), disrupting the interaction between the YY1 zinc finger region and DNA. These findings were supported by human data, including an observed negative correlation between YY1 gene expression and muscle fiber diameter. Collectively, GCN5 positively regulates muscle integrity through maintenance of structural protein expression via acetylation-dependent inhibition of YY1. This work implicates the role of protein acetylation in the regulation of muscle health and for consideration in the design of novel therapeutic strategies to support healthy muscle during myopathy or aging.
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