Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048824 | FEBS Letters | 2008 | 5 Pages |
Abstract
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 modification 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.
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Authors
Stefan R. Weisshaar, Kirstin Keusekotten, Anke Krause, Christiane Horst, Helen M. Springer, Kerstin Göttsche, R. Jürgen Dohmen, Gerrit J.K. Praefcke,