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. 2018 Jun 15;8:9168. doi: 10.1038/s41598-018-27601-z

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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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Regulation of the phosphorylation of B-RAF, RAF1, ERK1/2 and GC proliferation through the kinase PAKs. The granulosa cells were transfected with the reconstructed pYr-adshuttle-4-SLIT2 plasmids and co-infected with or without PAK1, PAK2 and PAK3 specific siRNA. (A) The phosphorylation levels of B-RAF and RAF1 proteins in the GCs with or without the specific siRNA interference were detected by western blotting and normalized for loading by comparison to the signal of β-actin. (B) The phosphorylation levels of the ERK1/2 proteins in the GCs with and without the specific siRNA interference were detected by western blotting and normalized for loading by comparison to the signal of β-actin. The signal intensity of the phosphorylated proteins was expressed as a ratio to the β-actin signal in arbitrary units (n = 10 per mean ± SEM). (C) Proliferation levels of the GCs with and without the specific siRNA interference were examined using an EdU Cell Proliferation Assay Kit. The statistical significance is indicated with different superscript characters (P < 0.01).