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Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing
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Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing
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Journal Article
Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing
2025
Overview
Cell cycle progression is governed by complexes of the cyclin-dependent kinases (CDKs) and their regulatory subunits cyclin and Cks1. CDKs phosphorylate hundreds of substrates, often at multiple sites. Multisite phosphorylation depends on Cks1, which binds initial priming phosphorylation sites to promote secondary phosphorylation at other sites. Here, we describe a similar role for a recently discovered phosphate-binding pocket (PP) on B-type cyclins. Mutation of the PP in Clb2, the major mitotic cyclin of budding yeast, alters bud morphology and delays the onset of anaphase. Mutation of the PP reduces multi-site phosphorylation of CDK substrates in vitro, including the Cdc16 and Cdc27 subunits of the anaphase-promoting complex/cyclosome and the Bud6 and Spa2 subunits of the polarisome. We conclude that the cyclin PP, like Cks1, controls the pattern of multisite phosphorylation on CDK substrates, thereby helping to establish the robust timing of cell-cycle events.
Cell cycle control depends on phosphorylation of many proteins by the kinase Cdk1. Here, the authors show that phosphorylation of Cdk1 substrates is influenced by a phosphate-binding pocket on the surface of the cyclin regulatory subunit.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/63
/ 82/58
/ 82/83
/ 96
/ Anaphase
/ Binding
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ Cyclin B
/ Cyclin-Dependent Kinases - genetics
/ Cyclin-Dependent Kinases - metabolism
/ Humanities and Social Sciences
/ Kinases
/ Mutation
/ Saccharomyces cerevisiae - cytology
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Science
/ Yeast
