C-terminal phosphorylation controls the stability and function of p27kip1.

@article{Kossatz2006CterminalPC,
  title={C-terminal phosphorylation controls the stability and function of p27kip1.},
  author={Uta Kossatz and J{\"o}rg Vervoorts and Irina Nickeleit and Holly A. Sundberg and James Simon Campbell Arthur and Michael P. Manns and Nisar Peter Malek},
  journal={The EMBO journal},
  year={2006},
  volume={25 21},
  pages={
          5159-70
        }
}
Entry of cells into the cell division cycle requires the coordinated activation of cyclin-dependent kinases (cdks) and the deactivation of cyclin kinase inhibitors. Degradation of p27kip1 is known to be a central component of this process as it allows controlled activation of cdk2-associated kinase activity. Turnover of p27 at the G1/S transition is regulated through phosphorylation at T187 and subsequent SCF(skp2)-dependent ubiquitylation. However, detailed analysis of this process revealed… CONTINUE READING
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