Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover.

@article{Winter2004ProteinKC,
  title={Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover.},
  author={Markus Winter and Diane Milne and Sylvia S Dias and Roman Kulikov and Uwe Knippschild and Christine Blattner and David C Meek},
  journal={Biochemistry},
  year={2004},
  volume={43 51},
  pages={16356-64}
}
Murine double-minute clone 2 protein (MDM2) is an E3 ubiquitin ligase that regulates the turnover of several cellular factors including the p53 tumor suppressor protein. As part of the mechanism of p53 induction in response to DNA damage, a cluster of serine residues within the central acidic domain of MDM2 become hypophosphorylated, leading to attenuation of MDM2-mediated p53 destruction. In the present study, we identify the protein kinase CK1delta as a major cellular activity that… CONTINUE READING
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