Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC.

@article{Li2002PhosphorylationBP,
  title={Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC.},
  author={P F Li and Jincheng Li and E Mueller and Albrecht Otto and Rainer Dietz and R{\"u}diger von Harsdorf},
  journal={Molecular cell},
  year={2002},
  volume={10 2},
  pages={247-58}
}
Caspases play a central role in apoptosis, but their activity is under the control of caspase-inhibiting proteins. A characteristic of caspase-inhibiting proteins is direct caspase binding. It is yet unknown how the localization of caspase-inhibiting proteins is regulated and whether there are upstream signals controlling their function. Here we report that the function of ARC is regulated by protein kinase CK2. ARC at threonine 149 is phosphorylated by CK2. This phosphorylation targets ARC to… CONTINUE READING

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