| Literature DB >> 29671337 |
Emma Bondy-Chorney1,1, Alix Denoncourt1,1, Yuka Sai1,1, Michael Downey1,1.
Abstract
Lysine acetylation is a critical post-translation modification that can impact a protein's localization, stability, and function. Originally thought to only occur on histones, we now know thousands of nonhistone proteins are also acetylated. In conjunction with many other proteins, lysine acetyltransferases (KATs) are incorporated into large protein complexes that carry out these modifications. In this review we focus on the contribution of two KATs, KAT2A and KAT2B, and their potential roles in the development and progression of cancer. Systems biology demands that we take a broad look at protein function rather than focusing on individual pathways or targets. As such, in this review we examine KAT2A/2B-directed nonhistone protein acetylations in cancer in the context of the 10 "Hallmarks of Cancer", as defined by Hanahan and Weinberg. By focusing on specific examples of KAT2A/2B-directed acetylations with well-defined mechanisms or strong links to a cancer phenotype, we aim to reinforce the complex role that these enzymes play in cancer biology.Entities:
Keywords: ATAC; Hallmarks of Cancer; KAT2A; KAT2B; SAGA; acetylation; acétylation; cancer; capacités distinctives du cancer; nonhistone
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Year: 2018 PMID: 29671337 DOI: 10.1139/bcb-2017-0297
Source DB: PubMed Journal: Biochem Cell Biol ISSN: 0829-8211 Impact factor: 3.626