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Biochem Cell Biol. 2019 Feb;97(1):30-45. doi: 10.1139/bcb-2017-0297. Epub 2018 Apr 19.

Nonhistone targets of KAT2A and KAT2B implicated in cancer biology 1.

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Department of Cellular and Molecular Medicine and Ottawa Institute of Systems Biology, 451 Smyth Rd., Ottawa, ON KIH 8M5, Canada.


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.


ATAC; Hallmarks of Cancer; KAT2A; KAT2B; SAGA; acetylation; ac├ętylation; cancer; capacit├ęs distinctives du cancer; nonhistone

[Indexed for MEDLINE]

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