Regulators, Cdc2 protein kinase

Figure 2. Regulators of the Cdc2 protein kinase. Schematic illustration of the regulators of Cdc2 kinase activity. Proteins that are circled indicate proteins that have been identified in higher eukaryotes only the squared proteins have been identified exclusively in the yeast systems. The remaining proteins have been identified in both higher and lower eukaryotes. Protein phosphatases are indicated by p tase.

Gould, K. L., and Nurse, P. (1989). Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 342 39-45. 

Hershko, A., Ganoth, D., Sudakin, V., Dahan, A., Cohen, L.H., Luca, F.C., Ruderman, J.V. and Eytan, E. (1994). Components of a system that ligates cyclin to ubiquitin and their regulation by protein kinase cdc2. J. Biol. Chem. 269,4940-4946. 

B. Regulators of Cdc2/Cdk2 Protein Kinase Activity Cyclins... 

Booher, R., and Beach, D. (1986). Site-specific mutagenesis of cdc2+, a cell cycle control gene of the fission yeast Schizosaccaromyces pombe. Mol. Cell. Biol. 6 3523-3530. Booher, R. N., Alfa, C. E., Hyams, J. S., and Beach, D. H. (1989). The fission yeast cdc2/cdcl3/sucl protein kinase regulation of catalytic activity and nuclear localization. CeU 58 485-497. 

Shuttleworth, J., Godfrey, R., and Colman, A. (1990). p40wo,J, a cdc2-related protein kinase involved in negative regulation of meiotic maturation of Xenopus oocytes. EMBOJ. 9 3233-3240. 

Simanis, V., and Nurse, R (1986). The cell cycle control gene cdc2+ of fission yeast encodes a protein kinase potentially regulated by phosphorylation. Cell 45 261-268. 

Fig. 13.5 P rinciples of regulation of cyclin-de-pendent protein kinases. The figure shows the principles of CDK regulation, usingthe CDC2 kinase (here simply referred to as CDK) as an example. The active form of CDK (a) is associated with the corresponding cyclin Thrl 60 of CDK (or equivalent positions in other CDKs) is phosphorylated, and Thrl4 and Tyrl 5 are unphosphorylated. Inactivation...

Fig. 7. Possible two-step regulation of protein function by proline-directed protein kinases and Pinl (a hypothesis) [63-65]. Phosphorylation (P) of some proteins on Ser/Thr-Pro sites by proline-directed kinases, such as cdc2 and MAP kinases, creates binding sites for Pinl. Pinl prefers to recognize the phosphorylated Ser/Thr-Pro with a hydrophobic amino acid (hy) stretch at the amino terminus, and it isomerizes the peptide bond adjacent to proline in the phosphorylated Ser/Thr-Pro sequence. This action of Pinl changes the shape of the whole protein from conformation 1 to conformation 2, which might have the ability to interact with other proteins, to translocate to other cellular compartments, or to change its life span. This regulation may be critical for the coordinated G,/M progression in mitosis.

---