USP3通过其去泛素化酶活性稳定p53蛋白。
USP3 stabilizes p53 protein through its deubiquitinase activity.
作者信息
Fu Song, Shao Shize, Wang Longqiang, Liu Haijun, Hou Haitao, Wang Yanan, Wang Huan, Huang Xiangpeng, Lv Renhua
机构信息
Department of Spine and Spinal Cord Surgery, Wendeng Orthopaedic Hospital, Weihai, Shandong, 264400, PR China.
Department of Neurology, The Affiliated Weihai Central Hospital of Weifang Medical College, Weihai, Shandong, 264400, PR China.
出版信息
Biochem Biophys Res Commun. 2017 Oct 14;492(2):178-183. doi: 10.1016/j.bbrc.2017.08.036. Epub 2017 Aug 12.
p53 is the guardian of the genome integrity and the degradation of p53 protein is mediated by MDM2. Here we report that USP3 interacts with p53 and regulates p53 stability. Depletion of USP3 lead to accelerated degradation of p53 in normal cells thereby enhanced cell proliferation and transformation. Reconstitution of wildtype USP3, but not the USP3 C168S mutant, restored the stability of p53 protein and inhibited cell proliferation and transformation. These findings suggest that USP3 is an important regulator of p53 and regulates normal cell transformation.
p53是基因组完整性的守护者，p53蛋白的降解由MDM2介导。在此我们报告，USP3与p53相互作用并调节p53的稳定性。USP3的缺失导致正常细胞中p53加速降解，从而增强细胞增殖和转化。野生型USP3（而非USP3 C168S突变体）的重建恢复了p53蛋白的稳定性，并抑制细胞增殖和转化。这些发现表明，USP3是p53的重要调节因子，并调节正常细胞转化。
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