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. 2017 Apr 26;7:1175. doi: 10.1038/s41598-017-01344-9

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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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p21 stability affects osteosarcoma cell proliferation. (A–C) Mutations of ubiquitination sites resulted in p21 accumulation in vivo. U2OS cells were transfected with p21-Flag or p21 mutants, including p21^K16R-Flag, p21^K75R-Flag, p21^K141R-Flag, p21^K154R-Flag, p21^K61R-Flag, p21^K163R-Flag, p21^{K154R K161R K163R}-Flag, p21^{K16R K161R K163R}-Flag, p21^{K16R K154R K163R}-Flag, p21^{K16R K154R K161R}-Flag, and p21^{K16R K154R K161R K163R}-Flag. After 48 h incubation, cells were lysed and immunoprecipitated with anti-p21, anti-CUL4B or β-Actin antibody. (B–D) Mutations of ubiquitination sites decreased cell proliferation. Cells used in (A and C) were applied to MTT assays to evaluate cell proliferation, and cell viability was determined at 490 nm.