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Dynamics of Cdk1 substrate specificity during the cell cycle.

Molecular cell | Jun 10, 2011

http://www.ncbi.nlm.nih.gov/pubmed/21658602

Cdk specificity is determined by the intrinsic selectivity of the active site and by substrate docking sites on the cyclin subunit. There is a long-standing debate about the relative importance of these factors in the timing of Cdk1 substrate phosphorylation. We analyzed major budding yeast cyclins (the G1/S-cyclin Cln2, S-cyclin Clb5, G2/M-cyclin Clb3, and M-cyclin Clb2) and found that the activity of Cdk1 toward the consensus motif increased gradually in the sequence Cln2-Clb5-Clb3-Clb2, in parallel with cell cycle progression. Further, we identified a docking element that compensates for the weak intrinsic specificity of Cln2 toward G1-specific targets. In addition, Cln2-Cdk1 showed distinct consensus site specificity, suggesting that cyclins do not merely activate Cdk1 but also modulate its active-site specificity. Finally, we identified several Cln2-, Clb3-, and Clb2-specific Cdk1 targets. We propose that robust timing and ordering of cell cycle events depend on gradual changes in the substrate specificity of Cdk1.

Pubmed ID: 21658602 RIS Download

Mesh terms: Amino Acid Motifs | Binding Sites | CDC2 Protein Kinase | Cell Cycle | Consensus Sequence | Hydrophobic and Hydrophilic Interactions | Models, Biological | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Substrate Specificity

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Associated grants

  • Agency: Wellcome Trust, Id: 079014/Z/06/Z
  • Agency: NIGMS NIH HHS, Id: R01 GM069901
  • Agency: Howard Hughes Medical Institute, Id:

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