APC/C-Cdh1-mediated degradation of the Polo kinase Cdc5 promotes the return of Cdc14 into the nucleolus

Clara Visintin, Brett N. Tomson, Rami Raha, Jennifer Paulson, Michael Cohen, Jack Taunton, Angelika Amon, Rosella Visintin

Research output: Contribution to journalArticlepeer-review

71 Scopus citations


In the budding yeast Saccharomyces cerevisiae, the protein phosphatase Cdc14 triggers exit from mitosis by promoting the inactivation of cyclin-dependent kinases (CDKs). Cdc14's activity is controlled by Cfi1/Net1, which holds and inhibits the phosphatase in the nucleolus from G1 until metaphase. During anaphase, two regulatory networks, the Cdc14 Early Anaphase Release (FEAR) network and the Mitotic Exit Network (MEN), promote the dissociation of Cdc14 from its inhibitor, allowing the phosphatase to reach its targets throughout the cell. The molecular circuits that trigger the return of Cdc14 into the nucleolus after the completion of exit from mitosis are not known. Here we show that activation of a ubiquitin ligase known as the Anaphase-Promoting Complex or Cyclosome (APC/C) bound to the specificity factor Cdh1 triggers the degradation of the Polo kinase Cdc5, a key factor in releasing Cdc14 from its inhibitor in the nucleolus.

Original languageEnglish (US)
Pages (from-to)79-90
Number of pages12
JournalGenes and Development
Issue number1
StatePublished - Jan 1 2008
Externally publishedYes


  • Cdc14
  • Cdc5
  • Cell cycle
  • Mitosis

ASJC Scopus subject areas

  • Medicine(all)


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