General Information:

Id: 5,241 (click here to show other Interactions for entry)
Diseases: Diabetes mellitus, type II - [OMIM]
Insulin resistance
Reference: Dominy JE Jr et al.(2010) Nutrient-dependent regulation of PGC-1alphas acetylation state and metabolic function through the enzymatic activities of Sirt1/GCN5 Biochim. Biophys. Acta 1804: 1676-1683 [PMID: 20005308]

Interaction Information:

Comment Sirtuin 1 (Sirt1) is a NAD+-dependent protein deacetylase that has been implicated in a panoply of physiological processes in mammals, including control of lipolytic rates in white adipose tissue, modulation of insulin secretion from pancreatic beta-cells, control of cytoplasmic and mitochondrial acetyl-CoA synthetase activity, regulation of the circadian clock, and regulation of the genetic response to various stressors such as heat shock, genotoxicity, and hypoxia. To this long list of biological functions, one can also add the regulation of PGC-1alpha acetylation state. Sirt1 has thus far been the only identified protein capable of binding to PGC-1alpha and deacetylating it both in vivo and in vitro. Sirt1 binds to a region of PGC-1alpha that is contained within amino acid residues 200–400 and deacetylates the protein in a NAD+-dependent manner.
Formal Description
Interaction-ID: 51105



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