Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Protein ubiquitylation

E2 enzymes: lessons in ubiquitin transfer from XLID patients

Nature Chemical Biology volume 15, pages 6–7 (2019)Cite this article

Subjects

Characterization of a novel mutation in the E2 ubiquitin-conjugating enzyme UBE2A accounts for the decreased activity of the mutant enzyme that underlies disease and provides important insight into the catalytic mechanism of E2s.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Fig. 1: UBE2A Q93E aminolysis activity can be recovered at high pH.

References

  1. Pickart, C. M. Annu. Rev. Biochem. 70, 503–533 (2001).

    Article  CAS  PubMed  Google Scholar 

  2. Stewart, M. D., Ritterhoff, T., Klevit, R. E. & Brzovic, P. S. Cell Res. 26, 423–440 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. de Oliveira, J. F. et al. Nat. Chem. Biol. https://doi.org/10.1038/s41589-018-0177-2 (2018).

    Article  Google Scholar 

  4. Kim, J. et al. Cell 137, 459–471 (2009).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Hibbert, R. G., Huang, A., Boelens, R. & Sixma, T. K. Proc. Natl Acad. Sci. USA 108, 5590–5595 (2011).

    Article  CAS  PubMed  Google Scholar 

  6. Nascimento, R. M., Otto, P. A., de Brouwer, A. P. & Vianna-Morgante, A. M. Am. J. Hum. Genet. 79, 549–555 (2006).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand

    Martina Foglizzo & Catherine L. Day

Authors
  1. Martina Foglizzo
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Catherine L. Day
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Catherine L. Day.

Ethics declarations

Competing interests

The authors declare no competing interests.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Foglizzo, M., Day, C.L. E2 enzymes: lessons in ubiquitin transfer from XLID patients. Nat Chem Biol 15, 6–7 (2019). https://doi.org/10.1038/s41589-018-0191-4

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/s41589-018-0191-4

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing