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Nature Reviews Molecular Cell Biology 10, 564-568 (August 2009) | doi:10.1038/nrm2707

OpinionAn additional role for SUMO in ubiquitin-mediated proteolysis

Marie-Claude Geoffroy1 & Ronald T. Hay1  About the authors

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Although the post-translational modification of proteins with small ubiquitin-like modifier (SUMO) has a role in many biological processes, it was thought that SUMO, unlike ubiquitin, does not target proteins for degradation. However, these views need to be revised, as recent findings in yeast and human cells indicate that SUMO can act as a signal for the recruitment of E3 ubiquitin ligases, which leads to the ubiquitylation and degradation of the modified protein.

Author affiliations

  1. Marie-Claude Geoffroy and Ronald T. Hay are at the Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, UK.

Correspondence to: Ronald T. Hay1 Email: r.t.hay@dundee.ac.uk

Published online 28 May 2009

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