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Biochim Biophys Acta. 2010 Aug;1804(8):1645-51. doi: 10.1016/j.bbapap.2009.12.021. Epub 2010 Jan 7.

Mitochondrial sirtuins.

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  • 1Gladstone Institute of Virology and Immunology, University of California, San Francisco, CA, USA.

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.

Copyright 2010 Elsevier B.V. All rights reserved.

PMID:
20060508
[PubMed - indexed for MEDLINE]
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