Figure 2 | Scientific Reports

Figure 2

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

Figure 2

Identification of the sites of SUMOylation in PIM1. (a) Schematic showing the kinase domain of PIM1, and the position of various lysine (K) and and glutamic acid (E) residues predicted to be involved in SUMOylation. (b) WT PIM1 or single amino acid substitution site mutants were expressed at near equal protein levels in COS7 cells with 6His-SUMO2, by transfecting different amounts of plasmids. Empty vector was included, where appropriate, to maintain equal amounts of transfected plasmid DNA. An aliquot of whole cell lysate was taken as input, and the remainder subjected to Ni2+-NTA pull-down to capture SUMOylated proteins. The samples were subjected to SDS-PAGE followed by western blotting using a PIM1 antibody.

Back to article page