Sirt1 is the most evolutionarily conserved mammalian sirtuin. It plays a vital role in the regulation of metabolism, stress responses, genome stability, and ultimately aging. Although much attention has focused on the identification of the cellular targets and functional networks controlled by Sirt1, the mechanisms that regulate Sirt1 activity by biological stimuli have only recently begun to emerge. As an enzyme, the activity of Sirt1 can be controlled by the availability of its substrates, post-translational modifications, interactions with other proteins, or changes in its expression levels. In this review, we briefly discuss the ways and means by which the activity of Sirt1 is fine-tuned under different conditions.
Published by Elsevier Ltd.