Figure 8 | Scientific Reports

Figure 8

From: A functional SUMO-motif in the active site of PIM1 promotes its degradation via RNF4, and stimulates protein kinase activity

Figure 8

Model for regulation of PIM1 by SUMOylation. The bi-lobed structure of PIM1 kinase is shown in blue. The consensus SUMOylated lysine residue is located in the substrate binding pocket (K169 in deep blue). For the purpose of presentation, the non-consensus lysine is shown in blue in the N-terminal domain. Stimuli such as growth factors or stress might induce SUMOylation of PIM1 under endogenous conditions. SUMOylated PIM1 can bind and phosphorylate substrates. Once this is achieved, a SUMO targeted ubiquitin ligase is recruited to polySUMOylated PIM1 leading to attachment of polyubiquitin chains on PIM1. The SUMOylated and ubiquitylated PIM1 is then targeted for degradation by the proteasome.

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