Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 12, Pages 1415-1424Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2706
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Funding
- Wellcome Trust [079014/Z/06/Z]
- European Molecular Biology Organization and Howard Hughes Medical Institute [1253]
- Estonian government [IUT2-21]
- American Cancer Society [RSG-12-131-01-CCG]
- Wellcome Trust [079014/Z/06/Z] Funding Source: Wellcome Trust
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The order and timing of cell-cycle events is controlled by changing substrate specificity and different activity thresholds of cyclin-dependent kinases (CDKs). However, it is not understood how a single protein kinase can trigger hundreds of switches in a sufficiently time-resolved fashion. We show that cyclin-Cdk1-Cks1-dependent phosphorylation of multisite targets in Saccharomyces cerevisiae is controlled by key substrate parameters including distances between phosphorylation sites, distribution of serines and threonines as phosphoacceptors and positioning of cyclin-docking motifs. The component mediating the key interactions in this process is Cks1, the phosphoadaptor subunit of the cyclin-Cdk1-Cks1 complex. We propose that variation of these parameters within networks of phosphorylation sites in different targets provides a wide range of possibilities for differential amplification of Cdk1 signals, thus providing a mechanism to generate a wide range of thresholds in the cell cycle.
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