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. 2017 Aug 8;7:7555. doi: 10.1038/s41598-017-08085-9

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© The Author(s) 2017

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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35 kDa variant of SG2NA has no role in cell cycle. (A) Cells stably overexpressing 35 kDa were harvested, 100 μg of total protein lysate was loaded on SDS-polyacrylamide gel and probed with SG2NA and β-actin. (B) 35 kDa overexpressing NIH3T3 cells were fractionated and organelle rich fractions loaded on SDS-polyacrlamide gel followed by western analysis using SG2NA antibody. (C) Representative FACS histograms of NIH3T3 cells stably transfected with 35 kDa SG2NA. (D) Graphical representation of the percentage of cells present in different phases of cell cycle during the cell cycle preogression. Error bars are the standard deviation of 3 independent experiments. (E) Schematic representation of proposed process. SG2NA remains in hyperphosphorylated state in the presence of okadoic acid. This hyperphosphorylated SG2NA is more stable. PD98059 inhibits phosphorylation of MAPK kinase and thus ERK. The decrease in phosphorylation of ERK results in decreased activity of ERK thereby decreasing inhibitory phosphorylation of GSK3β which inturn increases pSG2NA level thus increases its stability. LiCl is known to inhibit GSK3β activity by increasing its Ser-9 phosphorylation, thereby not phosphorylating SG2NA hence decreased level of SG2NA was observed. Full length blots for panel (A) are shown in Supplementary Figure S1.