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. 2011 Jun 17;286(31):27342–27349. doi: 10.1074/jbc.M111.220848

FIGURE 1.

FIGURE 1.

Influence of SUMOylation on protein phosphorylation. A, inhibition of SUMO modification by ginkgolic acid. HEK293T cells were treated with 100 μm ginkgolic acid or DMSO as a control for 6 h before harvest, then lysed and probed with anti-SUMO1 and SUMO2/3 antibody. Actin was used as a loading control. IB, immunoblotting. B, the same samples from A and pervanadate-treated samples were blotted with pan-anti-phospho-tyrosine antibody. Actin was used as a loading control. C, HEK293T cells were transfected with pcDNA3.0 control, HA-SUMO1, or HA-SUMO2 plasmids and were starved for 18 h after 24 h of transfection. Cells were then harvested, lysed, and blotted with anti-SUMO1, SUMO2/3, and HA antibodies. D, the same samples from C were blotted with pan-anti-phospho-tyrosine antibody. Actin was used as a loading control. E, SUMO1 or SUMO2/3 shRNA plasmids, as well as LacZ plasmid control, were transfected into HEK293T cells for 48 h. Cells were harvested, lysed, and blotted with anti-SUMO1 and SUMO2 antibody. Actin was used as a loading control. F, the same samples from A and E were blotted with anti-FAK and anti-pTyr-FAK antibody. Actin was used as a loading control. Pv, pervanadate.

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