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The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin

Nature Structural & Molecular Biology volume 19, pages 458460 (2012) | Download Citation

Abstract

SUMOylation promotes targeting of HP1α to pericentric heterochromatin. Here we identify the SUMO-specific protease SENP7 in mouse as a maintenance factor for HP1α accumulation at this location. SENP7 interacts directly with HP1α, localizes at HP1-enriched pericentric domains and can deconjugate SUMOylated HP1α in vivo. Depletion of SENP7 delocalizes HP1α from pericentric heterochromatin without affecting H3K9me3 levels. We propose that following targeting of HP1α, a subsequent deSUMOylation event enables HP1α retention at these domains.

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References

  1. 1.

    et al. Nucleic Acids Res. 19, 789–794 (1991).

  2. 2.

    & Mol. Cells 26, 217–227 (2008).

  3. 3.

    et al. Nat. Cell Biol. 12, 719–727 (2010).

  4. 4.

    & Nat. Rev. Genet. 8, 35–46 (2007).

  5. 5.

    et al. Nat. Genet. 43, 220–227 (2011).

  6. 6.

    & Biochim. Biophys. Acta 1792, 155–162 (2009).

  7. 7.

    J. Biol. Chem. 284, 8223–8227 (2009).

  8. 8.

    & Trends Biochem. Sci. 32, 286–295 (2007).

  9. 9.

    Trends Cell Biol. 17, 370–376 (2007).

  10. 10.

    & Biochem. J. 428, 133–145 (2010).

  11. 11.

    , , & Biochem. J. 421, 223–230 (2009).

  12. 12.

    et al. Nat. Genet. 30, 329–334 (2002).

  13. 13.

    et al. Cell 107, 323–337 (2001).

  14. 14.

    , , & Proc. Natl. Acad. Sci. USA 107, 15093–15098 (2010).

  15. 15.

    et al. J. Biol. Chem. 282, 26217–26224 (2007).

  16. 16.

    , , & J. Biol. Chem. 282, 1595–1606 (2007).

Download references

Acknowledgements

We thank R. Hay (University of Dundee) for reagents, C. Gazin for preliminary MS data, S. Cantaloube for technical help, A. vandenBerg for critical reading of the manuscript, members of the UMR218 unit for discussions and the Curie Imaging platform for microscopy facility. K. Romeo received support from Université Pierre et Marie Curie (UPMC) and Ministère de l'Enseignement Supérieur et de la Recherche. This work was supported by la Ligue Nationale contre le Cancer (Equipe labellisée Ligue 2010), the European Commission Network of Excellence EpiGeneSys (HEALTH-F4-2010-257082 to G.A.), European Research Council Advanced Grant 2009-AdG_20090506 “Eccentric” to G.A. and ANR “ECenS” ANR-09-BLAN-0257-01 to G.A.

Author information

Author notes

    • Christèle Maison
    •  & Kelly Romeo

    These authors contributed equally to this work.

Affiliations

  1. Institut Curie, Centre de Recherche, Paris, France.

    • Christèle Maison
    • , Kelly Romeo
    • , Delphine Bailly
    • , Marion Dubarry
    • , Jean-Pierre Quivy
    •  & Geneviève Almouzni
  2. Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche UMR218, Paris, France.

    • Christèle Maison
    • , Kelly Romeo
    • , Delphine Bailly
    • , Marion Dubarry
    • , Jean-Pierre Quivy
    •  & Geneviève Almouzni

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Contributions

J.-P.Q., C.M. and G.A. conceived and designed the experiments. K.R., C.M., D.B., M.D. and J.-P.Q. conducted the experiments. J.-P.Q., C.M., K.R. and G.A. analyzed the data. J.-P.Q., C.M. and G.A. wrote the paper.

Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Jean-Pierre Quivy or Geneviève Almouzni.

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DOI

https://doi.org/10.1038/nsmb.2244

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