Mitochondrial sirtuins |
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Authors: | Jing-Yi Huang Matthew D Hirschey Tadahiro Shimazu Linh Ho Eric Verdin |
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Institution: | Gladstone Institute of Virology and Immunology, University of California, San Francisco, CA, USA |
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Abstract: | 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. |
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Keywords: | Mitochondria Sirtuin SIRT3 SIRT4 SIRT5 O-Acetyl-ADP-ribose Acetylation |
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