USP7 controls Chk1 protein stability by direct deubiquitination.

@article{Vega2014USP7CC,
  title={USP7 controls Chk1 protein stability by direct deubiquitination.},
  author={Ignacio Alonso-de Vega and Y. San Pedro Mart{\'i}n and Veronique A. J. Smits},
  journal={Cell cycle},
  year={2014},
  volume={13 24},
  pages={
          3921-6
        }
}
Chk1, an essential checkpoint kinase in the DNA damage response pathway (DDR), is tightly regulated by both ATR-dependent phosphorylation and proteasome-mediated degradation. Here we identify ubiquitin hydrolase USP7 as a novel regulator of Chk1 protein stability. USP7 was shown before to regulate other DDR proteins such as p53, Hdm2 and Claspin, an adaptor protein in the ATR-Chk1 pathway required for Chk1 activation. Depletion or inhibition of USP7 leads to lower Chk1 levels. The decreased… CONTINUE READING
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