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. 2018 Jul 27;50(7):1–13. doi: 10.1038/s12276-018-0100-7

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — The KAT activity of ARD1 is regulated by PTMs. While autoacetylation at the K136 residue stimulates the KAT activity of ARD1, phosphorylation at the S228 residue inhibits the KAT activity of ARD1. Autoacetylation is conserved among ARD1 isoforms, including ARD1²³⁵ and ARD1²²⁵; however, autoacetylation regulates differential cellular functions depending on the isoform. While the autoacetylation of ARD1²³⁵ enhances cellular growth, the autoacetylation of ARD1²²⁵ inhibits angiogenesis. The KAT activity of ARD1 might also be regulated by unknown binding proteins