The Phosphatase Cdc14 Triggers Mitotic Exit by Reversal of Cdk-Dependent Phosphorylation
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This work shows that the Cdc14 phosphatase triggers mitotic exit by three parallel mechanisms, each of which inhibits Cdk activity, and induces degradation of mitotic cyclins.About:
This article is published in Molecular Cell.The article was published on 1998-12-01 and is currently open access. It has received 780 citations till now. The article focuses on the topics: Mitotic exit & Polo-like kinase.read more
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Functional homology among human and fission yeast Cdc14 phosphatases.
TL;DR: The results support a Cdc14 conserved inhibitory mechanism acting on S. pombe Cdc25 protein and suggest that human cells may regulate CDC25 in a similar manner to inactivate Cdk1-mitotic cyclin complexes.
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Molecular Mechanisms that Restrict Yeast Centrosome Duplication to One Event per Cell Cycle
Menattallah Elserafy,Mirela Šarić,Annett Neuner,Tien-chen Lin,Wanlu Zhang,Christian Seybold,Lavanya Sivashanmugam,Elmar Schiebel +7 more
TL;DR: It is shown that Sfi1 C-terminal domain harbors phosphorylation sites for Cdk1 and the polo-like kinase Cdc5, which inhibit SPB duplication as phosphomimetic sfi1 mutations lead to metaphase cells with a single SPB.
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Oscillations in Cdc14 release and sequestration reveal a circuit underlying mitotic exit
Romilde Manzoni,Francesca Montani,Clara Visintin,Fabrice Caudron,Andrea Ciliberto,Rosella Visintin +5 more
TL;DR: The phosphatase Cdc14 exerts negative feedback on its upstream regulators to limit its release from the nucleolus to once per cell cycle.
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Early expressed Clb proteins allow accumulation of mitotic cyclin by inactivating proteolytic machinery during S phase.
TL;DR: It is shown that the relationship between anaphase-promoting complex (APC) and Clb proteins is reversed in S phase such that the early Clb kinases inactivate APCHct1 to allow Clb2 accumulation.
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Big Lessons from Little Yeast: Budding and Fission Yeast Centrosome Structure, Duplication, and Function.
TL;DR: How analysis of fungal SPBs has advanced the understanding of centrosomes and NE events is reviewed, which involves events similar or identical to those needed for de novo nuclear pore complex assembly.
References
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Cyclin-dependent kinases: engines, clocks, and microprocessors.
TL;DR: This work has shown that Cdk activity is governed by a complex network of regulatory subunits and phosphorylation events whose precise effects on Cdk conformation have been revealed by recent crystallographic studies.
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SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.
TL;DR: Different skp1 mutants arrest cells in either G1 or G2, suggesting a connection between regulation of proteolysis in different stages of the cycle.
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How proteolysis drives the cell cycle
TL;DR: Proteolysis drives cell cycle progression not only by regulating CDK activity, but by directly influencing chromosome and spindle dynamics, and also how proteolysis may directly trigger the transition from metaphase to anaphase.
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F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex
TL;DR: The ubiquitination pathway for the Cdk inhibitor Sic1 is reconstituted using recombinant proteins and the constituents of the SCF complex are members of protein families, likely to serve as the prototype for a large class of E3s formed by combinatorial interactions of related family members.
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The Saccharomyces cerevisiae Cell Cycle
TL;DR: The bibliography is intended more as a guide to the literature than as a historically accurate record of the development of the field; the authors apologize to the earlier workers whose contributions thus get less explicit credit than they deserve.