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 Under high nutrient conditions and low intracellular NAD+ concentrations, PGC-1alpha is hyperacetylated by GCN5 and located within punctate nuclear bodies along with its transcription factor binding partners. In this state, the PGC-1alpha complex is effectively transcriptionally inactive. As cells are confronted with low nutrient availability, however, intracellular NAD+ levels increase and lead to an increase in the rate at which PGC-1alpha is deacetylated by Sirt1. The change in PGC-1alpha acetylation coincides with an increased occupancy of PGC-1alpha at the promoters of its target genes and an increase in transcriptional activation by remodeling of the local chromatin environment, by proteins such as p300, and greater interaction with general transcriptional machinery, facilitated by proteins such as the TRAP/Mediator complex.
Formal Description
Interaction-ID: 51091



increases_activity of



via deacetylation