AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Carles Cantó, Zachary Gerhart-Hines, Jerome N. Feige, Marie Lagouge, Lilia Noriega, Jill C. Milne, Peter J. Elliott, Pere Puigserver and Johan Auwerx ()
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Carles Cantó: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch, France
Zachary Gerhart-Hines: Harvard Medical School, Boston, Massachusetts 02115, USA
Jerome N. Feige: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch, France
Marie Lagouge: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch, France
Lilia Noriega: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch, France
Jill C. Milne: Sirtris Pharmaceuticals Inc., Cambridge, Massachusetts 02139, USA
Peter J. Elliott: Sirtris Pharmaceuticals Inc., Cambridge, Massachusetts 02139, USA
Pere Puigserver: Harvard Medical School, Boston, Massachusetts 02115, USA
Johan Auwerx: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch, France

Nature, 2009, vol. 458, issue 7241, 1056-1060

Abstract: Energy metabolism AMP-activated protein kinase (AMPK) is a cellular energy sensor that helps coordinate glucose and lipid metabolism. Here, AMPK is shown to transcriptionally regulate genes involved in controlling energy metabolism in skeletal muscle by acting together with the NAD+-dependent deacetylase SIRT1. AMPK enhances SIRT1 activity by increasing cellular NAD+ levels. This results in the deacetylation and activation of the SIRT1 downstream target PGC-1α.

Date: 2009
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DOI: 10.1038/nature07813

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