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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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Schematic diagram of the CRL4B^DCAF11 ubiquitin complex in human osteosarcoma cells. CUL4B serves as a scaffold that binds to adaptor protein DDB1 and the substrate receptor protein DCAF11 at the N terminus and interacts with RING protein RBX1 at the C terminus, thereby forming the CRL4B E3 ligase. The CRL4B E3 ligase can promote ubiquitin transfer from RBX1-bound E2 to the specific substrate p21 in osteosarcoma cells, leading to p21 ubiquitination. The degradation of p21 diminishes the inhibition of CDK2, thereby resulting in cell cycle arrest at S phase.