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Visintin, C, Tomson, BN, Rahal, R, Paulson, J, Cohen, M, Taunton, J, Amon, A and Visintin, R (2008) APC/C-Cdh1-mediated degradation of the Polo kinase Cdc5 promotes the return of Cdc14 into the nucleolus. Genes Dev. 22:79-90


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.


PubMed PMC2151016 Online version:10.1101/gad.1601308


Alleles; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Cell Nucleolus/enzymology; Endopeptidases/metabolism; Metaphase; Microscopy, Fluorescence; Mitosis; Models, Biological; Nuclear Proteins; Protein Biosynthesis; Protein Kinases/genetics; Protein Kinases/metabolism; Protein Tyrosine Phosphatases/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/metabolism; Ubiquitin-Protein Ligase Complexes/metabolism



Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status



GO:2000060: positive regulation of ubiquitin-dependent protein catabolic process

ECO:0000314: direct assay evidence used in manual assertion


Seeded From UniProt


See also


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