The Mitotic Exit Network and Cdc14 phosphatase initiate cytokinesis by counteracting CDK phosphorylations and blocking polarised growth

Alberto Sanchez-Diaz, Pedro Junior Nkosi, Stephen Murray, Karim Labib (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)

    Abstract

    Polarisation of the actin cytoskeleton must cease during cytokinesis, to support efficient assembly and contraction of the actomyosin ring at the site of cell division, but the underlying mechanisms are still understood poorly in most species. In budding yeast, the Mitotic Exit Network (MEN) releases Cdc14 phosphatase from the nucleolus during anaphase, leading to the inactivation of mitotic forms of cyclin-dependent kinase (CDK) and the onset of septation, before G1-CDK can be reactivated and drive re-polarisation of the actin cytoskeleton to a new bud. Here, we show that premature inactivation of mitotic CDK, before release of Cdc14, allows G1-CDK to divert the actin cytoskeleton away from the actomyosin ring to a new site of polarised growth, thereby delaying progression through cytokinesis. Our data indicate that cells normally avoid this problem via the MEN-dependent release of Cdc14, which counteracts all classes of CDK-mediated phosphorylations during cytokinesis and blocks polarised growth. The dephosphorylation of CDK targets is therefore central to the mechanism by which the MEN and Cdc14 initiate cytokinesis and block polarised growth during late mitosis.
    Original languageEnglish
    Pages (from-to)3620-3634
    Number of pages15
    JournalEMBO Journal
    Volume31
    Issue number17
    DOIs
    Publication statusPublished - 29 Aug 2012

    Keywords

    • Protein Tyrosine Phosphatases
    • Cell Cycle Proteins
    • Phosphorylation
    • Saccharomycetales
    • Mitosis
    • Cytokinesis
    • Cyclin-Dependent Kinases
    • Fungal Proteins

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