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. 2019 Aug 19;8(8):930. doi: 10.3390/cells8080930

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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c-Src-mediated phosphorylation of HDAC3 affects its enzymatic activity. Mutations of Y328 and Y331 on HDAC3 inhibited its enzymatic activity. 293T cells were transfected with plasmids encoding either HA-tagged HDAC3^WT or HA-tagged HDAC3^Y328/331A. Cell extracts were immunoprecipitated with anti-HA antibody and assayed for histone deacetylase (HDAC) activity. The results were expressed as fold changes in optical density (OD) values relative to OD values of control (HA-HDAC3-overexpressing cells). The values presented are the means ± SD of three independent experiments.