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PARP1 and CBP lose their footing in cancer

Nature Structural & Molecular Biology volume 21, pages 947948 (2014) | Download Citation

The human histone macroH2A.1.1 recruits activated PARP1 enzyme to chromatin through its poly(ADP-ribose)-binding macrodomain. New work shows that PARP1 and CBP can be displaced from chromatin in cancer cells that have lost macroH2A.1.1, thus leading to changes in histone H2B acetylation at cancer-relevant genes.

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References

  1. 1.

    & Cell 144, 646–674 (2011).

  2. 2.

    & Cancer Cell 22, 9–20 (2012).

  3. 3.

    & Nat. Rev. Drug Discov. 13, 337–356 (2014).

  4. 4.

    Nature 488, 148–150 (2012).

  5. 5.

    , , , & Nat. Genet. 22, 323–324 (1999).

  6. 6.

    & Science 257, 1398–1400 (1992).

  7. 7.

    , , & J. Cell Biol. 147, 1399–1408 (1999).

  8. 8.

    et al. Oncogene 28, 3423–3428 (2009).

  9. 9.

    et al. Nature 468, 1105–1109 (2010).

  10. 10.

    et al. Nat. Struct. Mol. Biol. 19, 1139–1146 (2012).

  11. 11.

    , , , & Nat. Struct. Mol. Biol. 12, 624–625 (2005).

  12. 12.

    et al. EMBO J. 24, 1911–1920 (2005).

  13. 13.

    , , & Science 336, 728–732 (2012).

  14. 14.

    & Nat. Rev. Mol. Cell Biol. 13, 411–424 (2012).

  15. 15.

    et al. Nat. Struct. Mol. Biol. 19, 685–692 (2012).

  16. 16.

    et al. Nat. Struct. Mol. Biol. 16, 923–929 (2009).

  17. 17.

    & Am. J. Pathol. 180, 2516–2526 (2012).

  18. 18.

    , , & EMBO J. 30, 2373–2387 (2011).

  19. 19.

    et al. Mol. Cell. Biol. 32, 1442–1452 (2012).

  20. 20.

    et al. Nat. Struct. Mol. Biol. 21, 981–989 (2014).

Download references

Acknowledgements

We acknowledge support from the Deutsche Forschungsgemeinschaft to G.T. (TI817/2-1) and to A.G.L. (SFB1064 Chromatin Dynamics), and we thank C. Laverty for comments.

Author information

Affiliations

  1. Gyula Timinszky and Andreas G. Ladurner are at the Department of Physiological Chemistry, Butenandt Institute and Ludwig-Maximilians-University Biomedical Center, Ludwig-Maximilians-University of Munich, Munich, Germany.

    • Gyula Timinszky
    •  & Andreas G Ladurner
  2. Andreas Ladurner is also at the International Max Planck Research School for Molecular and Cellular Life Sciences, Martinsried, Germany, the Center for Integrated Protein Science Munich (CIPSM), Munich, Germany, and the Munich Cluster for Systems Neurology (SyNergy), Munich, Germany.

Authors

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Competing interests

Andreas Ladurner is on the Scientific Advisory Board of VolitionRx.

Corresponding author

Correspondence to Andreas G Ladurner.

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DOI

https://doi.org/10.1038/nsmb.2913

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