Mitochondrial sirtuins

作者：Huang, Jing-Yi; Hirschey, Matthew D.; Shimazu, Tadahiro; Ho, Linh; Verdin, Eric^*

来源：Biochimica et Biophysica Acta-Proteins and Proteomics, 2010, 1804(8): 1645-1651.

DOI：10.1016/j.bbapap.2009.12.021

• Mitochondria
• Sirtuin
• SIRT3
• SIRT4
• SIRT5
• O-Acetyl-ADP-ribose
• Acetylation

Sirtuins have emerged as important proteins in aging, stress resistance and metabolic regulation. Three sirtuins, SIRT3, 4 and 5, are located within the mitochondrial matrix. SIRT3 and SIRT5 are NAD(+)-dependent deacetylases that remove acetyl groups from acetyllysine-modified proteins and yield 2'-O-acetyl-ADP-ribose and nicotinamide. SIRT4 can transfer the ADP-ribose group from NAD(+) onto acceptor proteins. Recent findings reveal that a large fraction of mitochondrial proteins are acetylated and that mitochondrial protein acetylation is modulated by nutritional status. This and the identification of targets for SIRT3, 4 and 5 support the model that mitochondrial sirtuins are metabolic sensors that modulate the activity of metabolic enzymes via protein deacetylation or mono-ADP-ribosylation. Here, we review and discuss recent progress in the study of mitochondrial sirtuins and their targets.

• 出版日期2010-8