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Nature Cell Biology 10, 507 - 509 (2008)
doi:10.1038/ncb0508-507
Marked for death
Kevin Petrie1 & Arthur Zelent1
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Kevin Petrie and Arthur Zelent are in the Section of Haemato-Oncology, Institute of Cancer Research, 15 Cotswold Road, Sutton, Surrey SM2 5NG, UK.
e-mail: arthur.zelent@icr.ac.uk
Abstract
SUMOylation of PML–RAR
oncoprotein has been linked to its arsenic-induced degradation and the therapeutic response in acute promyelocytic leukaemia. Two groups identify PML as an in vivo target of the RING finger ubiquitin E3 ligase RNF4, which specifically binds polySUMOylated PML and is essential for the arsenic-induced catabolism of both PML and PML–RAR.
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RESEARCH
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradationNature Cell Biology Article (01 May 2008)
Arsenic degrades PML or PML?RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathwayNature Cell Biology Article (01 May 2008)
The deubiquitinylation and localization of PTEN are regulated by a HAUSP?PML networkNature Letters to Editor (09 Oct 2008)
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