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• W1976421909 abstract "Myocardin belongs to the SAF-A/B, Acinus, PIAS (SAP) domain family of transcription factors and is specifically expressed in cardiac and smooth muscle. Myocardin functions as a transcriptional coactivator of SRF and is sufficient and necessary for smooth muscle gene expression. We have previously found that myocardin induces the acetylation of nucleosomal histones surrounding SRF-binding sites in the control regions of cardiac and smooth muscle genes through recruiting chromatin-modifying enzyme p300, yet no studies have determined whether myocardin itself is similarly modified. In this study, we show that myocardin is a direct target for p300-mediated acetylation. p300 acetylates lysine residues at the N terminus of the myocardin protein. Interestingly, a direct interaction between p300 and myocardin, which is mediated by the C terminus of myocardin, is required for the acetylation event. Acetylation of myocardin by p300 enhances the association of myocardin and SRF as well as the formation of the myocardin-SRF-CArG box ternary complex. Conversely, acetylation of myocardin decreases the binding of histone deacetylase 5 (HDAC5) to myocardin. Acetylation of myocardin is required for myocardin to activate smooth muscle genes. Our study demonstrates that acetylation plays a key role in modulating myocardin function in controlling cardiac and smooth muscle gene expression." @default.
• W1976421909 created "2016-06-24" @default.
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• W1976421909 date "2012-11-01" @default.
• W1976421909 modified "2023-09-28" @default.
• W1976421909 title "Acetylation of Myocardin Is Required for the Activation of Cardiac and Smooth Muscle Genes" @default.
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• W1976421909 doi "https://doi.org/10.1074/jbc.m112.353649" @default.
• W1976421909 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3493894" @default.
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