Identification and characterization of the novel protein CCDC106 that interacts with p53 and promotes its degradation.

Jianlin Zhou, Xi Qiao, Ling Xiao, Wei Sun, Lin Wang, Hong Li, Yuan Wu, Xiaofeng Ding, Xiang Hu, Chang Zhou, Jian Zhang

Key Laboratory of Protein Chemistry and Developmental Biology of Education Ministry of China, College of Life Science, Hunan Normal University, Changsha, Hunan, China.

FEBS letters 2010 Mar 19

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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. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Jianlin Zhou, Xi Qiao, Ling Xiao, Wei Sun, Lin Wang, Hong Li, Yuan Wu, Xiaofeng Ding, Xiang Hu, Chang Zhou, Jian Zhang. Identification and characterization of the novel protein CCDC106 that interacts with p53 and promotes its degradation. FEBS letters. 2010 Mar 19;584(6):1085-90