// Marta Di Martile 1 , Donatella Del Bufalo 1 and Daniela Trisciuoglio 1 1 Preclinical Models and New Therapeutic Agents Unit, Research, Advanced Diagnostics and Technological Innovation Department, Regina Elena National Cancer Institute, Rome, Italy Correspondence to: Daniela Trisciuoglio, email: // Keywords : lysine acetylation, lysine acetyltransferases, KAT inhibitors, cancer Received : May 20, 2016 Accepted : June 01, 2016 Published : June 14, 2016 Abstract Lysine acetylation is a post-translational modification that regulates gene transcription by targeting histones as well as a variety of transcription factors in the nucleus. Recently, several reports have demonstrated that numerous cytosolic proteins are also acetylated and that this modification, affecting protein activity, localization and stability has profound consequences on their cellular functions. Interestingly, most non-histone proteins targeted by acetylation are relevant for tumorigenesis. In this review, we will analyze the functional implications of lysine acetylation in different cellular compartments, and will examine our current understanding of lysine acetyltransferases family, highlighting the biological role and prognostic value of these enzymes and their substrates in cancer. The latter part of the article will address challenges and current status of molecules targeting lysine acetyltransferase enzymes in cancer therapy.
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Martile et al. (2016) studied this question.