GSK-3 beta targets Cdc25A for ubiquitin-mediated proteolysis, and GSK-3 beta inactivation correlates with Cdc25A overproduction in human cancers.

@article{Kang2008GSK3BT,
  title={GSK-3 beta targets Cdc25A for ubiquitin-mediated proteolysis, and GSK-3 beta inactivation correlates with Cdc25A overproduction in human cancers.},
  author={Tiebang Kang and Yongkun Wei and Yuchi Honaker and Hiroshi Yamaguchi and Ettore Appella and M -C Hung and Helen Piwnica-Worms},
  journal={Cancer cell},
  year={2008},
  volume={13 1},
  pages={36-47}
}
The Cdc25A phosphatase positively regulates cell-cycle transitions, is degraded by the proteosome throughout interphase and in response to stress, and is overproduced in human cancers. The kinases targeting Cdc25A for proteolysis during early cell-cycle phases have not been identified, and mechanistic insight into the cause of Cdc25A overproduction in human cancers is lacking. Here, we demonstrate that glycogen synthase kinase-3beta (GSK-3beta) phosphorylates Cdc25A to promote its proteolysis… CONTINUE READING
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