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Whi5 hypo- and hyper-phosphorylation dynamics control cell cycle entry and progression.

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    Cell cycle progression relies on cyclin-dependent kinase (CDK) phosphorylation of Whi5, a key regulator of the G1/S transition in budding yeast. This study reveals how Whi5 phosphorylation controls cell cycle timing and progression through multiple phases.

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    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Genetics

    Background:

    • Cell cycle progression is tightly regulated by cyclin-dependent kinases (CDKs) phosphorylating key substrates.
    • In budding yeast, Whi5 is a critical transcriptional inhibitor controlling the G1/S transition by inhibiting the SBF complex.

    Approach:

    • Identified 19 phosphorylation sites on Whi5.
    • Determined which sites mediate G1 hypo-phosphorylation and late-G1 hyper-phosphorylation.
    • Investigated the role of priming sites in docking Cks1 for Cdk1-Cln1,2 complexes.

    Key Points:

    • Mutation of 7 G1 hypo-phosphorylation sites delayed the G1/S transition and increased cell size.
    • Whi5 hyper-phosphorylation depends on priming sites for Cks1 docking.
    • Hyper-phosphorylation is essential for Whi5 nuclear export and SBF target gene expression.

    Conclusions:

    • Whi5 phosphorylation regulates the G1/S transition by controlling its nuclear localization and inhibitory function.
    • Proper Whi5 phosphorylation is required for timely progression through G1, S, G2, and M phases, not just G1.
    • This study elucidates the molecular mechanisms of Whi5 phosphorylation and its broader role in cell cycle regulation.