Key Laboratory of Protein Chemistry and Developmental Biology of Education Ministry of China, College of Life Science, Hunan Normal University, Changsha, Hunan, China.
FEBS Lett. 2010 Mar 19;584(6):1085-90. doi: 10.1016/j.febslet.2010.02.031. Epub 2010 Feb 14.
The putative CCDC106 protein was previously identified as a p53-interacting partner by automated yeast two-hybrid screening, but its sequence and function have not been validated experimentally. Here, we identified three variant transcripts of the CCDC106 gene; these transcripts differ in their second exons due to the use of different splice acceptor site, but encode an identical protein of 280 residues. A bipartite nuclear localisation signal at residues 151-164 mediates the nuclear localisation of CCDC106. Double immunofluorescence staining revealed the colocalisation of endogenous CCDC106 and p53 protein in nuclei. The in vivo interaction between CCDC106 and p53 was confirmed by a co-immunoprecipitation assay. Furthermore, we demonstrated that CCDC106 promotes the degradation of p53 protein and inhibits its transactivity.
假定的 CCDC106 蛋白先前通过自动酵母双杂交筛选被鉴定为 p53 相互作用伙伴,但它的序列和功能尚未通过实验验证。在这里,我们鉴定了 CCDC106 基因的三个变体转录本;由于使用不同的剪接受体位点,这些转录本在其二号外显子上存在差异,但编码相同的 280 个残基的蛋白质。位于残基 151-164 的二分核定位信号介导 CCDC106 的核定位。双免疫荧光染色显示内源性 CCDC106 和 p53 蛋白在核内共定位。通过共免疫沉淀测定证实了 CCDC106 与 p53 之间的体内相互作用。此外,我们证明 CCDC106 促进 p53 蛋白的降解并抑制其转录活性。