Journal
PHARMACOLOGICAL RESEARCH
Volume 62, Issue 1, Pages 35-41Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.phrs.2009.12.006
Keywords
SIRT1; NAD; Deacetylation; Metabolic homeostasis
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Funding
- Ecole Polytechnique Federale de Lausanne (EPFL)
- National Science Foundation of Switzerland
- NIH [DK59820]
- European Research Council Ideas programme [ERC-2008-AdG-23118]
- FEBS
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The biological function of most proteins relies on reversible post-translational modifications, among which phosphorylation is most prominently studied and well recognized. Recently, a growing amount of evidence indicates that acetylation-deacetylation reactions, when applied to crucial mediators, can also robustly affect the function of target proteins and thereby have wide-ranging physiological impacts. Sirtuin 1 (SIRT1), which functions as a nicotinamide adenine dinucleotide (NAD(+))-dependent protein deacetylase, deacetylates a wide variety of metabolic molecules in response to the cellular energy and redox status and as such causes significant changes in metabolic homeostasis. This review surveys the evidence for the emerging role of SIRT1-mediated deacetylation in the control of metabolic homeostasis. (C) 2009 Elsevier Ltd. All rights reserved.
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