p40MO15 associates with a p36 subunit and requires both nuclear translocation and Thr176 phosphorylation to generate cdk-activating kinase activity in Xenopus oocytes.

@article{Labb1994p40MO15AW,
  title={p40MO15 associates with a p36 subunit and requires both nuclear translocation and Thr176 phosphorylation to generate cdk-activating kinase activity in Xenopus oocytes.},
  author={J-C. Labb{\'e} and A. Marina Martinez and Didier Fesquet and J. P. Capony and Josephine Darbon and Jean Derancourt and Alain Devault and Nathalie Morin and Jean-claude Cavadore and Marcel Dor{\'e}e},
  journal={The EMBO journal},
  year={1994},
  volume={13 21},
  pages={5155-64}
}
p40MO15, a cdc2-related protein, is the catalytic subunit of the kinase (CAK, cdk-activating kinase) responsible for Thr161/Thr160 phosphorylation and activation of cdk1/cdk2. We have found that strong overexpression of p40MO15 only moderately increases CAK activity in Xenopus oocytes, indicating that a regulatory CAK subunit (possibly a cyclin-like protein) limits the ability to generate CAK activity in p40MO15 overexpressing oocytes. This 36 kDa subunit was microsequenced after extensive… CONTINUE READING

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