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. 2018 Oct 8;7(10):80. doi: 10.1038/s41389-018-0091-1

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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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Fig. 2 — a Expression of Vav1 in NIH3T3 cells stably transfected with pcDNA3, Vav1, and oncVav1 and the mutants E59K, D517E, and L801P was analyzed. Cells were treated with 25 μM of the proteasome inhibitor MG132 for 4 h or were left untreated. Cell lysates were immunoblotted with anti-Vav1 and anti-actin antibodies. b D517E is a highly stable protein. The half-life of Vav1 mutant proteins was measured by using CHX to block new protein synthesis. NIH3T3 cells stably expressing pcDNA3, Vav1, oncVav1, E59K, D517E, and L801P were treated with 100 μg/ml CHX for the indicated time periods. Cells were immunoblotted using anti-Vav1 and anti-actin antibodies. Results were quantified with the ImageJ program. c The histogram presents the mean time required for each protein to reach its half-life calculated by using http://www.calculator.net/half-life-calculator.html. Calculation was made for several time points. Error bars are indicated