Several ubiquitin E3 ligases are regulated by SUMOylation (reviewed in Wilson and Heaton 2008). SUMOylation appears to be necessary for nuclear import of MDM2, the E3 ligase that ubiquitinylates TP53 (p53). SUMOylation of VHL abolishes its ubiquitin ligase activity. HERC2, RNF168, and BRCA1 are ubiquitin ligases that are SUMOylated during DNA damage response and repair.
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PML TRIM27, PIAS1, and PIAS2-1 can each SUMOylate MDM2 with SUMO1 at lysine-182 (Miyauchi et al. 2002, Chu and Yang 2011). An unSUMOylatable mutant of MDM2 accumulates in the cytosol so SUMOylation may be part of the process of nuclear import of MDM2 (Miyauchi et al. 2002).
PIAS4 SUMOylates VHL at lysine-159, lysine-171, and lysine-196 with SUMO1 (Cai et al. 2010, Cai and Robertson 2010, Chien et al. 2013). SUMOylation facilitates the oligomerization of VHL, abolishes the inhibitory function of VHL on HIF1A, and abolishes the tumor suppressor function of VHL by inactivating the ubiquitinylation activity of VHL.
RANBP2 of the nuclear pore complex SUMOylates MDM2 with SUMO1 at lysine-182 (Mayauchi et al. 2002). An unSUMOylatable mutant of MDM2 accumulates in the cytosol so SUMOylation may be part of the process of nuclear import of MDM2 (Miyauchi et al. 2002).
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