CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.

@article{Miyata2004CK2CM,
  title={CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.},
  author={Yoshihiko Miyata and Eisuke Nishida},
  journal={Molecular and cellular biology},
  year={2004},
  volume={24 9},
  pages={4065-74}
}
Cdc37 is a kinase-associated molecular chaperone whose function in concert with Hsp90 is essential for many signaling protein kinases. Here, we report that mammalian Cdc37 is a pivotal substrate of CK2 (casein kinase II). Purified Cdc37 was phosphorylated in vitro on a conserved serine residue, Ser13, by CK2. Moreover, Ser13 was the unique phosphorylation site of Cdc37 in vivo. Crucially, the CK2 phosphorylation of Cdc37 on Ser13 was essential for the optimal binding activity of Cdc37 toward… CONTINUE READING

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