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. 2019 Feb 26;9:2814. doi: 10.1038/s41598-019-39116-2

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© The Author(s) 2019

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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H89 effects on Myl12b and Scyl2 phosphorylation. Examples of phosphosites from Myl12b and Scyl2 are shown along with their associated linear models. Concentration of H89 (log₁₀ scale) is plotted against log₂-transformed intensity normalized for the batch effect. Dark red lines correspond to fitted linear models with slopes equal to β_H89 and intercepts averaged from 3 replicates. UniProt accession numbers, gene symbols, phosphorylation positions, and centralized amino acid sequences are shown on the top. Phosphorylation at T19 and S20 in myosin regulatory light chain (Myl12b) are seen to be significantly decreased by H89 treatment in both PKA-intact (a) and PKA-null cells (b). Phosphorylation at S677 in SCY1-like protein 2 (Scly2) is inhibited by H89 in PKA-intact cells (c), but not in PKA-null cells (d), suggesting that this phosphosite is a PKA target.