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Protein deacetylation by SIRT1: An emerging key post-translational modification in metabolic regulation

期刊

PHARMACOLOGICAL RESEARCH
卷 62, 期 1, 页码 35-41

出版社

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.phrs.2009.12.006

关键词

SIRT1; NAD; Deacetylation; Metabolic homeostasis

资金

  1. Ecole Polytechnique Federale de Lausanne (EPFL)
  2. National Science Foundation of Switzerland
  3. NIH [DK59820]
  4. European Research Council Ideas programme [ERC-2008-AdG-23118]
  5. FEBS

向作者/读者索取更多资源

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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