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Sumoylation

Centre of attention

Nature Reviews Molecular Cell Biology volume 4, page 340 (2003)Cite this article

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The single sumoylation motif in CtBP hinted to David Wotton's group that CtBP could be sumoylated. In vitro, CtBP sumoylation minimally required recombinant E1 (an activating enzyme), Ubc9 and SUMO-1. In vivo, CtBP immunoprecipitated from HeLa cells was detected with an anti-SUMO-1-specific antibody. Lysine 428 of CtBP was identified as the principal site for SUMO conjugation, and the surrounding motif was important for efficient sumoylation.

CtBP can be nuclear and cytoplasmic but, in the presence of recombinant Pc2, much of it colocalized with Pc2 in nuclear foci, where it was found to be sumoylated. Pc2 itself was also sumoylated, so could Pc2 affect SUMO localization? Co-expressing Pc2 caused SUMO-1 and Ubc9 to move to nuclear foci. Pc2 colocalized there, too, suggesting that these foci were probably PcG bodies.

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References

ORIGINAL RESEARCH PAPER

  1. Kagey, M. H., Melhuish, T. A. & Wotton, D. The Polycomb protein Pc2 is a SUMO E3. Cell 113, 127–137 (2003)

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FURTHER READING

  1. Muller, S. et al. SUMO, ubiquitin's mysterious cousin. Nature Rev. Mol. Cell Biol. 2, 202–210 (2001)

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Authors
  1. Katrin Bussell
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David Wotton's laboratory

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Bussell, K. Centre of attention. Nat Rev Mol Cell Biol 4, 340 (2003). https://doi.org/10.1038/nrm1117

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  • DOI: https://doi.org/10.1038/nrm1117

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