Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase

Mardo Kõivomägi, Ervin Valk, Rainis Venta, Anna Iofik, Martin Lepiku, Eva Rose M. Balog, Seth M. Rubin, David O. Morgan and Mart Loog ()
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Mardo Kõivomägi: Institute of Technology, University of Tartu
Ervin Valk: Institute of Technology, University of Tartu
Rainis Venta: Institute of Technology, University of Tartu
Anna Iofik: Institute of Technology, University of Tartu
Martin Lepiku: Institute of Technology, University of Tartu
Eva Rose M. Balog: University of California
Seth M. Rubin: University of California
David O. Morgan: University of California
Mart Loog: Institute of Technology, University of Tartu

Nature, 2011, vol. 480, issue 7375, 128-131

Abstract: Proteins as complex switches Multisite phosphorylation of a protein can allow an ultra-sensitive switch-like response. For example, in the yeast cyclin-dependent kinase (Cdk) inhibitor Sic1, it can lead to its rapid destruction and the initiation of S-phase of the cell cycle. Kõivomägi et al. demonstrate that multisite phosphorylations of Sic1 are not random events, but are part of a specific phosphorylation cascade catalysed by two different Cdk–cyclin complexes, with initial priming phosphorylations followed by docking-dependent phosphorylation events. Such an intricate mechanism may also apply to other kinase targets with multiple phosphorylation sites.

Date: 2011
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DOI: 10.1038/nature10560

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