Abstract
Protein N-ε-lysine acetylation is is an important post-translational modification that plays critical roles in the regulation of many cellular processes. A role for this modification in the process of aging goes back two decades to the discovery that the yeast NAD+-dependent histone deacetylase Sir2 regulates lifespan in yeast. While the Sirtuin family of protein deacetylases has been intensively studied in many model systems and is definitively linked to aging, the enzymes responsible for protein acetylation, protein acetyltransferases (KATs), have not received a similar level of attention. However, a series of recent studies have directly explored the role of specific KATs in aging. These studies have shown that modulation of KAT activity can influence cellular pathways important for aging and directly effect organismal lifespan.
Highlights
Protein N-ε-lysine acetyltransferases (KATs) are a diverse family of enzymes [10]
The idea that protein acetylation plays an important role in the regulation of aging began with the pioneering work on the Sirtuin family of NAD+-dependent protein deacetylases
Hat1 was the first KAT identified. It was originally isolated based on its role in the evolutionarily conserved diacetylation of newly synthesized histone H4 during the process of chromatin assembly [12,13]
Summary
Protein N-ε-lysine acetyltransferases (KATs) are a diverse family of enzymes [10]. While many of these enzymes were originally identified as histone acetyltransferases, it is clear that most, if not all, have multiple substrates. The idea that protein acetylation plays an important role in the regulation of aging began with the pioneering work on the Sirtuin family of NAD+-dependent protein deacetylases. Subsequent studies in model organisms such as, flies, worms and mice, showed that genetic or pharmacological modulation of Sirtuin activity influenced lifespan [3,4,5,6,7,8,9]. Protein N-ε-lysine acetyltransferases (KATs) are a diverse family of enzymes [10].
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