Journal
FEBS LETTERS
Volume 582, Issue 21-22, Pages 3174-3178Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.08.008
Keywords
small ubiquitin-like modifier; ubiquitin; relatively interesting new gene finger; protein degradation; promyelocytic leukemia
Funding
- EU [MERG-CT-2004-006344]
- Deutsche Forschungsgemeinschaft [SFB635]
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We have recently reported that poly-SUMO-2/3 conjugates are subject to a ubiquitin-dependent proteolytic control in human cells. Here we show that arsenic trioxide (ATO) increases SUMO-2/3 modification of promyelocytic leukemia (PML) leading to its subsequent ubiquitylation in vivo. The SUMO-binding ubiquitin ligase RNF4 mediates this modi. cation and causes disruption of PML nuclear bodies upon treatment with ATO. Reconstitution of SUMO-dependent ubiquitylation of PML by RNF4 in vitro and in a yeast trans vivo system revealed a preference of RNF4 for chain forming SUMOs. Polysumoylation of PML in response to ATO thus leads to its recognition and ubiquitylation by RNF4. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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