Marked for death

SUMOylation of PML–RARα oncoprotein has been linked to its arsenic-induced degradation and the therapeutic response in acute promyelocytic leukaemia. Two groups identify PML as an in vivo target of the RING finger ubiquitin E3 ligase RNF4, which specifically binds polySUMOylated PML and is essential for the arsenic-induced catabolism of both PML and PML–RARα.

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Figure 1: A hypothetical pathway highlighting the role of RNF4 in controlling PML stability in normal cells and in response to ATO-induced PML degradation.

References

  1. 1

    Dilda, P. J. & Hogg, P. J. Cancer Treat Rev. 33, 542–564 (2007).

    CAS  Article  Google Scholar 

  2. 2

    Zhu, J. et al. Proc. Natl Acad. Sci. USA 94, 3978–3983 (1997).

    CAS  Article  Google Scholar 

  3. 3

    Kamitani, T. et al. J. Biol. Chem. 273, 26675–26682 (1998).

    CAS  Article  Google Scholar 

  4. 4

    Lallemand-Breitenbach, V. et al. J. Exp. Med. 193, 1361–1371 (2001).

    CAS  Article  Google Scholar 

  5. 5

    Lallemand-Breitenbach, V. et al. Nature Cell Biol. 10, 547–555 (2008).

    CAS  Article  Google Scholar 

  6. 6

    Tatham, M. H. et al. Nature Cell Biol. 10, 538–546 (2008).

    CAS  Article  Google Scholar 

  7. 7

    Matic, I. et al. Mol. Cell Proteomics 7, 132–144 (2008).

    CAS  Article  Google Scholar 

  8. 8

    Mukhopadhyay, D. et al. J. Cell Biol. 174, 939–949 (2006).

    CAS  Article  Google Scholar 

  9. 9

    Hayakawa, F. & Privalsky, M. L. Cancer Cell 5, 389–401 (2004).

    CAS  Article  Google Scholar 

  10. 10

    Reineke, E. L. et al. Mol. Cell Biol. 28, 997–1006 (2008).

    CAS  Article  Google Scholar 

  11. 11

    Poukka, H., Aarnisalo, P., Santti, H., Janne, O. A. & Palvimo, J. J. J. Biol. Chem. 275, 571–579 (2000).

    CAS  Article  Google Scholar 

  12. 12

    Fedele, M. et al. J. Biol. Chem. 275, 7894–7901 (2000).

    CAS  Article  Google Scholar 

  13. 13

    Lyngso, C. et al. J. Biol. Chem. 275, 26144–26149 (2000).

    CAS  Article  Google Scholar 

  14. 14

    Kaiser, F. J., Moroy, T., Chang, G. T., Horsthemke, B. & Ludecke, H. J. J. Biol. Chem. 278, 38780–38785 (2003).

    CAS  Article  Google Scholar 

  15. 15

    Wu, S. M. et al. Mol. Pharmacol. 66, 1317–1324 (2004).

    CAS  Article  Google Scholar 

  16. 16

    Shyu, H. W., Hsu, S. H., Hsieh-Li, H. M. & Li, H. Exp. Cell Res. 287, 301–313 (2003).

    CAS  Article  Google Scholar 

  17. 17

    Wang, Z. G. et al. Science 279, 1547–1551 (1998).

    CAS  Article  Google Scholar 

  18. 18

    Hecker, C. M., Rabiller, M., Haglund, K., Bayer, P. & Dikic, I. J. Biol. Chem. 281, 16117–16127 (2006).

    CAS  Article  Google Scholar 

Download references

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Petrie, K., Zelent, A. Marked for death. Nat Cell Biol 10, 507–509 (2008). https://doi.org/10.1038/ncb0508-507

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