Cdc37: a protein kinase chaperone?

@article{Hunter1997Cdc37AP,
  title={Cdc37: a protein kinase chaperone?},
  author={Tony Hunter and Randy YC Poon},
  journal={Trends in cell biology},
  year={1997},
  volume={7 4},
  pages={157-61}
}
The activity of most protein kinases is highly regulated, typically via phosphorylation and/or subunit association. However, the folding of protein kinases into an active state or a form capable of activation is now emerging as another important step through which they can be regulated. The 50-kDa protein Cdc37 and the associated heat-shock protein Hsp90 have been found to bind to, and be required for the activity of, diverse protein kinases, including Cdk4, v-Src, Raf and SEVENLESS. Together… CONTINUE READING

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