Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability.

@article{Gresko2005CovalentMO,
  title={Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability.},
  author={Ekaterina Gresko and Andreas M{\"o}ller and Ana Roscic and M Lienhard Schmitz},
  journal={Biochemical and biophysical research communications},
  year={2005},
  volume={329 4},
  pages={
          1293-9
        }
}
The HIPK2 protein is a critical regulator of apoptosis and functionally interacts with p53 to increase gene expression. Here we show that human HIPK2 is modified by sumoylation at lysine 25, as revealed by in vivo and in vitro experiments. While SUMO-1 modification of HIPK2 has no influence on its ability to phosphorylate p53 at serine 46, to induce gene expression, and to mediate apoptosis, a non-sumoylatable HIPK2 mutant displays a strongly increased protein stability. The N-terminal SUMO-1… CONTINUE READING

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