Protein deacetylation by SIRT1: an emerging key post-translational modification in metabolic regulation.
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.
Yu
Jiujiu
J
Laboratory of Integrative and Systems Physiology (LISP) at the Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Auwerx
Johan
J
D000107:Acetylation; D000818:Animals; D004734:Energy Metabolism / Q000502:physiology*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D056564:Sirtuin 1 / Q000378:metabolism / Q000502:physiology*; D014157:Transcription Factors / Q000378:metabolism
D014157:Transcription Factors; C447939:SIRT1 protein, human; D056564:Sirtuin 1