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- W4321768021 abstract "Ordered protein phosphorylation by CDKs is a key mechanism for regulating the cell cycle. How temporal order is enforced in mammalian cells remains unclear. Using a fixed cell kinase assay and phosphoproteomics, we show how CDK1 activity and non-catalytic CDK1 subunits contribute to the choice of substrate and site of phosphorylation. Increases in CDK1 activity alter substrate choice, with intermediate- and low-sensitivity CDK1 substrates enriched in DNA replication and mitotic functions, respectively. This activity dependence is shared between Cyclin A- and Cyclin B-CDK1. Cks1 has a proteome-wide role as an enhancer of multisite CDK1 phosphorylation. Contrary to the model of CDK1 as an exclusively proline-directed kinase, we show that Cyclin A and Cks1 enhance non-proline-directed phosphorylation, preferably on sites with a +3 lysine residue. Indeed, 70% of cell-cycle-regulated phosphorylations, where the kinase carrying out this modification has not been identified, are non-proline-directed CDK1 sites." @default.
- W4321768021 created "2023-02-25" @default.
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- W4321768021 creator A5075478076 @default.
- W4321768021 creator A5080078780 @default.
- W4321768021 date "2023-03-01" @default.
- W4321768021 modified "2023-10-06" @default.
- W4321768021 title "Cyclin A and Cks1 promote kinase consensus switching to non-proline-directed CDK1 phosphorylation" @default.
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- W4321768021 doi "https://doi.org/10.1016/j.celrep.2023.112139" @default.
- W4321768021 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36840943" @default.
- W4321768021 hasPublicationYear "2023" @default.
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