Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379.

@article{Lovly2008RegulationOC,
  title={Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379.},
  author={Christine M Lovly and Ling Yan and Christine E. Ryan and Saeko Takada and Helen Piwnica-Worms},
  journal={Molecular and cellular biology},
  year={2008},
  volume={28 19},
  pages={5874-85}
}
The Chk2 protein kinase protects genome integrity by promoting cell cycle arrest or apoptosis in response to DNA double-strand breaks, and Chk2 mutations are found in both familial and sporadic cancers. Exposure of cells to ionizing radiation (IR) or radiomimetic drugs induces Chk2 phosphorylation by ATM, followed by Chk2 oligomerization, auto-/transphosphorylation, and activation. Here we demonstrate that Chk2 is ubiquitinated upon activation and that this requires Chk2 kinase activity. Serine… CONTINUE READING

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