Regulation of the Chk2 protein kinase by oligomerization-mediated cis- and trans-phosphorylation.

@article{Schwarz2003RegulationOT,
  title={Regulation of the Chk2 protein kinase by oligomerization-mediated cis- and trans-phosphorylation.},
  author={Julie K. Schwarz and Christine M Lovly and Helen Piwnica-Worms},
  journal={Molecular cancer research : MCR},
  year={2003},
  volume={1 8},
  pages={598-609}
}
Chk2 is a serine/threonine protein kinase found mutated in certain hereditary and sporadic cancers. Ionizing radiation (IR) activates the kinase activity of Chk2 in a phosphorylation-dependent manner. ATM phosphorylates Chk2 on threonine 68, which promotes oligomerization and phosphorylation on threonines 383 and 387 within the activation loop of the catalytic domain. In this study, threonines 68, 383, and 387 were confirmed as sites of Chk2 phosphorylation both in vitro and in vivo. In… CONTINUE READING

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