AROuSing SIRT1: Identification of a Novel Endogenous SIRT1 Activator Eric Verdin  Molecular Cell  Volume 28, Issue 3, Pages 354-356 (November 2007) DOI: 10.1016/j.molcel.2007.10.013 Copyright © 2007 Elsevier Inc. Terms and Conditions

Figure 1 AROS-Dependent Regulation of SIRT1 Enzymatic Activity The N terminus of SIRT1 regulates the enzymatic activity of its NAD-dependent deacetylase via interaction with AROS. This newly identified factor may act alone, in synergy with an unidentified cofactor, or by suppressing the binding of an inhibitory factor. The SIRT1 N-terminal domain is also the site of action of resveratrol, a small molecule activator of SIRT1 enzymatic activity. SIRT1 utilizes NAD+ to deacetylate several cellular proteins, including p53, NF-κB, PGC-1α, HIV Tat, and the FOXO transcription factors, and to modulate the cellular response to a variety of stresses, including fasting, DNA damage, and infection. Molecular Cell 2007 28, 354-356DOI: (10.1016/j.molcel.2007.10.013) Copyright © 2007 Elsevier Inc. Terms and Conditions