Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Sir2 is a NAD(+)-dependent histone deacetylase that controls gene silencing, cell cycle, DNA damage repair, and life span. Prompted by the observation that the [NAD(+)]/[NADH] ratio is subjected to dynamic fluctuations in skeletal muscle, we have tested whether Sir2 regulates muscle gene expression and differentiation. Sir2 forms a complex with the acetyltransferase PCAF and MyoD and, when overexpressed, retards muscle differentiation. Conversely, cells with decreased Sir2 differentiate prematurely. To inhibit myogenesis, Sir2 requires its NAD(+)-dependent deacetylase activity. The [NAD(+)]/[NADH] ratio decreases as muscle cells differentiate, while an increased [NAD(+)]/[NADH] ratio inhibits muscle gene expression. Cells with reduced Sir2 levels are less sensitive to the inhibition imposed by an elevated [NAD(+)]/[NADH] ratio. These results indicate that Sir2 regulates muscle gene expression and differentiation by possibly functioning as a redox sensor. In response to exercise, food intake, and starvation, Sir2 may sense modifications of the redox state and promptly modulate gene expression.
- National Institute of Arthritis and Musculoskeletal and Skin Diseases United States
- National Institutes of Health United States
- National Institute of Health Pakistan
- National Institutes of Health Malaysia
- Children’s National Health System United States
Saccharomyces cerevisiae Proteins, Muscle Fibers, Skeletal, Gene Expression Regulation, Developmental, Cell Differentiation, Cell Biology, NAD, Cell Line, Repressor Proteins, Mice, Sirtuin 2, Acetyltransferases, Animals, Humans, Sirtuins, Muscle, Skeletal, Molecular Biology, Oxidation-Reduction, Histone Acetyltransferases, MyoD Protein
Saccharomyces cerevisiae Proteins, Muscle Fibers, Skeletal, Gene Expression Regulation, Developmental, Cell Differentiation, Cell Biology, NAD, Cell Line, Repressor Proteins, Mice, Sirtuin 2, Acetyltransferases, Animals, Humans, Sirtuins, Muscle, Skeletal, Molecular Biology, Oxidation-Reduction, Histone Acetyltransferases, MyoD Protein
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