Dataset Information

Re-examining the role of Cdc14 phosphatase in mitotic exit

ABSTRACT: Given that Cdc14 enzymes are so highly conserved, we questioned whether budding yeast Cdc14 could really have such a different influence on Cdk site dephosphorylation. We used quantitative phosphoproteomics to directly measure the in vivo specificity of budding yeast Cdc14 and found that it very selectively dephosphorylates a distinct sub-class of Cdk sites and does not catalyze widespread Cdk site dephosphorylation as widely believed.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Brendan Powers

LAB HEAD: Mark Hall

PROVIDER: PXD005237 | Pride | 2017-07-13

REPOSITORIES: Pride

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Publications

Re-examining the role of Cdc14 phosphatase in reversal of Cdk phosphorylation during mitotic exit.

Powers Brendan L BL Hall Mark C MC

Journal of cell science 20170629 16

Inactivation of cyclin-dependent kinase (Cdk) and reversal of Cdk phosphorylation are universally required for mitotic exit. In budding yeast (<i>Saccharomyces cerevisiae</i>), Cdc14 is essential for both and thought to be the major Cdk-counteracting phosphatase. However, Cdc14 is not required for mitotic exit in many eukaryotes, despite highly conserved biochemical properties. The question of how similar enzymes could have such disparate influences on mitotic exit prompted us to re-examine the ...[more]

PMID: 28663385

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Project description:This model is from the article: Downregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic exit in budding yeast. Queralt E, Lehane C, Novak B, Uhlmann F. Cell. 2006 May 19;125(4):719-32. 16713564 , Abstract: After anaphase, the high mitotic cyclin-dependent kinase (Cdk) activity is downregulated to promote exit from mitosis. To this end, in the budding yeast S. cerevisiae, the Cdk counteracting phosphatase Cdc14 is activated. In metaphase, Cdc14 is kept inactive in the nucleolus by its inhibitor Net1. During anaphase, Cdk- and Polo-dependent phosphorylation of Net1 is thought to release active Cdc14. How Net1 is phosphorylated specifically in anaphase, when mitotic kinase activity starts to decline, has remained unexplained. Here, we show that PP2A(Cdc55) phosphatase keeps Net1 underphosphorylated in metaphase. The sister chromatid-separating protease separase, activated at anaphase onset, interacts with and downregulates PP2A(Cdc55), thereby facilitating Cdk-dependent Net1 phosphorylation. PP2A(Cdc55) downregulation also promotes phosphorylation of Bfa1, contributing to activation of the "mitotic exit network" that sustains Cdc14 as Cdk activity declines. These findings allow us to present a new quantitative model for mitotic exit in budding yeast. This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2012 The BioModels.net Team. For more information see the terms of use . To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

Dataset Information

Re-examining the role of Cdc14 phosphatase in mitotic exit

Publications

Re-examining the role of Cdc14 phosphatase in reversal of Cdk phosphorylation during mitotic exit.

Similar Datasets

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