SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation

Matthew D. Hirschey, Tadahiro Shimazu, Eric Goetzman, Enxuan Jing, Bjoern Schwer, David B. Lombard, Carrie A. Grueter, Charles Harris, Sudha Biddinger, Olga R. Ilkayeva, Robert D. Stevens, Yu Li, Asish K. Saha, Neil B. Ruderman, James R. Bain, Christopher B. Newgard, Robert V. Farese, Frederick W. Alt, C. Ronald Kahn and Eric Verdin ()
Additional contact information
Matthew D. Hirschey: Gladstone Institute of Virology and Immunology, San Francisco, California 94158, USA
Tadahiro Shimazu: Gladstone Institute of Virology and Immunology, San Francisco, California 94158, USA
Eric Goetzman: The Children’s Hospital of Pittsburgh, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15201, USA
Enxuan Jing: Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215, USA
Bjoern Schwer: Gladstone Institute of Virology and Immunology, San Francisco, California 94158, USA
David B. Lombard: Howard Hughes Medical Institute, Program in Cellular and Molecular Medicine, The Children’s Hospital, Immune Disease Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
Carrie A. Grueter: Gladstone Institute of Cardiovascular Disease, University of California, San Francisco, California 94158, USA
Charles Harris: Gladstone Institute of Cardiovascular Disease, University of California, San Francisco, California 94158, USA
Sudha Biddinger: Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215, USA
Olga R. Ilkayeva: Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, North Carolina 27704, USA
Robert D. Stevens: Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, North Carolina 27704, USA
Yu Li: Cell Signaling Technology, Danvers, Massachusetts 01923, USA
Asish K. Saha: Physiology, and Biophysics and the Diabetes Unit, Boston University Medical Center, Boston, Massachusetts 02118, USA
Neil B. Ruderman: Physiology, and Biophysics and the Diabetes Unit, Boston University Medical Center, Boston, Massachusetts 02118, USA
James R. Bain: Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, North Carolina 27704, USA
Christopher B. Newgard: Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, North Carolina 27704, USA
Robert V. Farese: Gladstone Institute of Cardiovascular Disease, University of California, San Francisco, California 94158, USA
Frederick W. Alt: Howard Hughes Medical Institute, Program in Cellular and Molecular Medicine, The Children’s Hospital, Immune Disease Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
C. Ronald Kahn: Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215, USA
Eric Verdin: Gladstone Institute of Virology and Immunology, San Francisco, California 94158, USA

Nature, 2010, vol. 464, issue 7285, 121-125

Abstract: SIRT3 regulation of fatty acid oxidation The sirtuin family of regulatory proteins has been implicated in various biological pathways including responses to calorie restriction and metabolic stress. Work in mice now shows that sirtuin 3 (SIRT3), which mediates deacetylation of several mitochondrial proteins, is induced in liver and brown adipose tissue during fasting. One of SIRT3's substrates is shown to be long-chain acyl co-enzyme A dehydrogenase (LCAD). Without SIRT3, LCAD becomes hyperacetylated, which diminishes its activity, and reduces fatty acid oxidation. Mice without SIRT3 have all the hallmarks of fatty acid oxidation disorders during fasting, including reduced ATP levels and intolerance to cold. These findings suggest that acetylation is a novel regulatory mechanism for fatty acid oxidation.

Date: 2010
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DOI: 10.1038/nature08778

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