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Significance Many oxidative stimuli engage the 66-kDa Src homology 2 domain-containing protein (p66Shc) to induce reactive oxygen species (ROS). ROS regulated by p66Shc promotes aging and contributes to cancer, diabetes, obesity, cardiomyopathy, and atherosclerosis. Here we identify a fundamental mechanism that controls p66Shc and p66Shc-regulated ROS. We show that p66Shc is lysine acetylated when cells are faced with an oxidative stimulus (diabetes), and lysine acetylation of p66Shc is obligatory for p66Shc-induced ROS. In addition, lysine-acetylated p66Shc is deacetylated by the Sirtuin1 lysine deacetylase, and Sirt1-mediated deacetylation of p66Shc curtails ROS production. This intersection between p66Shc and Sirtuin1 adds a dimension to how p66Shc is regulated by certain stimuli and how Sirtuin1 suppresses oxidative stress promoted by such stimuli.

Sirtuin1-regulated lysine acetylation of p66Shc governs diabetes-induced vascular oxidative stress and endothelial dysfunction