RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

By M. Tatham, M. Geoffroy, Lin-nan Shen, Anna Plechanovová, N. Hattersley, E. Jaffray, J. Palvimo, R. Hay. Nature Cell Biology, 2008

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Targeting the ubiquitin system in cancer therapy (2009, background): “RNF4 has an important role in APL, as it recognizes SUMOylated PML as well as the APL-associated oncogenic fusion protein PML–RAR-α, and triggers their polyubiquitin-dependent proteasomal degradatio”
The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition (2010, background): “The presence of multiple SIMs in these ubiquitin ligases is noteworthy because tandem SIMs could recognize two or more SUMO molecules in a SUMO chai”
Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, background): “RNF4 possesses at least three closely spaced SIMs and shows a clear preference for substrates that are modified by a SUMO chain or at least three SUMO moieties [143].”
Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway (2008, methodology): “Although we have only detected ubiquitin conjugated to PML, another study published in this issue provides evidence for SUMO–ubiquitin conjugate”