期刊
ONCOGENE
卷 35, 期 1, 页码 69-82出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2015.63
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资金
- Freie und Hansestadt Hamburg
- Bundesministerium fur Gesundheit (BMG)
- Peter und Traudl Engelhorn Stiftung
- Erich und Gertrud Roggenbuck Stiftung
- Else Kroner-Fresenius-Stiftung
- Deutsche Krebshilfe e. V.
- Deutsche Forschungsgemeinschaft (DFG)
- Wilhelm Sander-Stiftung
- B Braun Stiftung
- Drager Stiftung
- Fonds der Chemischen Industrie
- Canadian Institutes of Health Research
- Canadian Foundation for Innovation (CFI)
- Ministere du Developpement economique, innovation et exportation Quebec (MDEIE)
- Cancer Research UK [13067] Funding Source: researchfish
Although modulation of the cellular tumor-suppressor p53 is considered to have the major role in E1A/E1B-55K-mediated tumorigenesis, other promyelocytic leukemia nuclear body (PML-NB)/PML oncogenic domain (POD)-associated factors including SUMO, Mre11, Daxx, as well as the integrity of these nuclear bodies contribute to the transformation process. However, the biochemical consequences and oncogenic alterations of PML-associated E1B-55K by SUMO-dependent PML-IV and PML-V interaction have so far remained elusive. We performed mutational analysis to define a PML interaction motif within the E1B-55K polypeptide. Our results showed that E1B-55K/PML binding is not required for p53, Mre11 and Daxx interaction. We also observed that E1B-55K lacking subnuclear PML localization because of either PML-IV or PML-V-binding deficiency was no longer capable of mediating E1B-55K-dependent SUMOylation of p53, inhibition of p53-mediated transactivation or efficiently transforming primary rodent cells. These results together with the observation that E1B-55K-dependent SUMOylation of p53 is required for efficient cell transformation, provides evidence for the idea that the SUMO ligase activity of the E1B-55K viral oncoprotein is intimately linked to its growth-promoting oncogenic activities.
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