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.
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Pickart, C. M. Annu. Rev. Biochem. 70, 503–533 (2001).
Stewart, M. D., Ritterhoff, T., Klevit, R. E. & Brzovic, P. S. Cell Res. 26, 423–440 (2016).
de Oliveira, J. F. et al. Nat. Chem. Biol. https://doi.org/10.1038/s41589-018-0177-2 (2018).
Kim, J. et al. Cell 137, 459–471 (2009).
Hibbert, R. G., Huang, A., Boelens, R. & Sixma, T. K. Proc. Natl Acad. Sci. USA 108, 5590–5595 (2011).
Nascimento, R. M., Otto, P. A., de Brouwer, A. P. & Vianna-Morgante, A. M. Am. J. Hum. Genet. 79, 549–555 (2006).
The authors declare no competing interests.
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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