Abstract
The posttranslational lysine acetylation of proteins is increasingly appreciated as a key regulatory mechanism in fundamental cellular process such as transcription, cytoskeleton dynamics, metabolic flux, and cell survival/death signaling. As empirical studies are undertaken to dissect the functional importance of specific acetylation events, methods for rapid detection of this modification on individual proteins, in different cellular contexts, is essential. Much like nucleosomal histones, the tumor suppressor protein p53 is acetylated on a number of distinct lysine residues, often with distinct functional consequences. We discuss here a number of technical considerations that facilitate the use of protein-specific antibodies to interrogate these key acetylation events.