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Modification of histone proteins by serotonin in the nucleus

The function of histone proteins can be modified through addition or removal of certain chemical groups. The addition of a serotonin molecule is a newly found histone modification that could influence gene expression.
  1. Marlene Cervantes

    1. Marlene Cervantes is at the Center for Epigenetics and Metabolism, U1233 INSERM, University of California Irvine, Irvine, California 92697, USA.

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  2. Paolo Sassone-Corsi

    1. Paolo Sassone-Corsi is at the Center for Epigenetics and Metabolism, U1233 INSERM, University of California Irvine, Irvine, California 92697, USA.

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Epigenetics has been defined as the study of heritable traits that do not involve changes in the DNA sequence. This view has been broadened by an avalanche of biochemical evidence revealing a complex and versatile array of molecular mechanisms that regulate gene expression without changing DNA sequences. These include chemical modifications of DNA and RNA molecules, as well as post-translational modifications of histones — the proteins around which DNA coils to form chromatin strands. Post-translational modifications of histones include acetylation, phosphorylation and methylation (addition of acetyl, phosphate and methyl groups, respectively) at specific amino-acid residues of these proteins1. Writing in Nature, Farrelly et al.2 report that histones can also be modified by the addition of serotonin, a molecule with essential roles in regulating neuron activity.

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Nature 567, 464-465 (2019)

doi: https://doi.org/10.1038/d41586-019-00532-z

References

  1. Borrelli, E., Nestler, E. J., Allis, C. D. & Sassone‑Corsi, P. Neuron 60, 961–974 (2008).

    Article  PubMed  Google Scholar 

  2. Farrelly, L. A. et al. Nature https://doi.org/10.1038/s41586-019-1024-7 (2019).

    Article  Google Scholar 

  3. Daubert, E. A. & Condron, B. G. Trends Neurosci. 33, 424–434 (2010).

    Article  PubMed  Google Scholar 

  4. Holloway, T. & Gonzalez-Maeso, J. ACS Chem. Neurosci. 6, 1099–1109 (2015).

    Article  PubMed  Google Scholar 

  5. Watts, S. W., Priestley, J. R. & Thompson, J. M. PLoS ONE 4, e5682 (2009).

    Article  PubMed  Google Scholar 

  6. Paulmann, N. et al. PLoS Biol. 7, e1000229 (2009).

    Article  PubMed  Google Scholar 

  7. Walther, D. J. et al. Cell 115, 851–862 (2003).

    Article  PubMed  Google Scholar 

  8. Sileno, S. et al. J. Proteomics 96, 314–327 (2014).

    Article  PubMed  Google Scholar 

  9. Csaba, G. & Kovacs, P. Cell Biol. Int. 30, 861–865 (2006).

    Article  PubMed  Google Scholar 

  10. Tessarz, P. & Kouzarides, T. Nature Rev. Mol. Cell Biol. 15, 703–708 (2014).

    Article  PubMed  Google Scholar 

  11. Greer, E. L. & Shi, Y. Nature Rev. Genet. 13, 343–357 (2012).

    Article  PubMed  Google Scholar 

  12. Karmodiya, K. et al. BMC Genom. 13, 424 (2012).

    Article  Google Scholar 

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