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

2. 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  , DOI: ( /j.molcel )
Copyright © 2007 Elsevier Inc. Terms and Conditions