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. 2017 Nov 10;7:15311. doi: 10.1038/s41598-017-15497-0

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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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NPRL2 and NPRL3 are nucleo-cytoplasmic proteins. (a) GFP signal HEK293 cells stably expressing FLAG-NPRL2-GFP (left panel) or NPRL3-GFP (right panel) was observed in the cells without treatment (NT) or in the cells treated with cycloheximide or MG132 at indicated concentrations and time. Scale bar is 5 μm. (b) Treatment with cycloheximide reduces NPRL2 protein level, but does not change NPRL3 expression. Whole cell lysates from the cells stably expressing FLAG-NPRL2-GFP or NPRL3-GFP and treated with cycloheximide for indicated time were analyzed by Western blotting with anti-GFP antibody to detect appropriate GATOR1 component and with anti-β-actin as a loading control. The protein level in % was calculated by normalizing the GFP signal to a corresponding β-actin signal and represented as a graph. The signal in the samples without treatment was set at 100%. Error bars represent the standard deviation in three independent experiments. (c). Treatment with MG132 induces NPRL2 stability. The analysis of cells treated with 20 μM MG132 for indicated time was done as in (b).