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The Phosphatase Cdc14 Triggers Mitotic Exit by Reversal of Cdk-Dependent Phosphorylation

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TLDR
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.
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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.

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Citations
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Journal ArticleDOI

Positive feedback sharpens the anaphase switch.

TL;DR: It is demonstrated that the cyclin-dependent kinase 1 (Cdk1)-dependent phosphorylation of securin near its destruction-box motif inhibits Securin ubiquitination by the APC, and that mutations that disruptSecurin phosphoregulation decrease the synchrony of chromosome segregation.
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Protein kinase Cdc15 activates the Dbf2-Mob1 kinase complex

TL;DR: The mechanisms that underlie activation of the protein kinase Dbf2 are investigated and it is proposed that Mob1 promotes this activation process by enabling Cdc15 to phosphorylate the critical Ser-374 and Thr-544 phosphoacceptor sites of DBF2.
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Complete loss of the tumor suppressor MAD2 causes premature cyclin B degradation and mitotic failure in human somatic cells.

TL;DR: It is found that severe reduction of MAD2 protein levels results in mitotic failure and extensive cell death arising from defective spindle formation, incomplete chromosome condensation, and premature mitotic exit leading to multinucleation.
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Phosphorylation by Cyclin B-Cdk Underlies Release of Mitotic Exit Activator Cdc14 from the Nucleolus

TL;DR: A regulatory circuit exists to ensure that the arbiter of the mitotic state, Cdk, sets in motion events that culminate in exit from mitosis and sustain the proper timing of late mitotic events.
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The nucleolus: the magician's hat for cell cycle tricks

TL;DR: The nucleolus, for decades considered a ribosome factory and site for ribosomal RNA synthesis and processing, has recently acquired new fame afteralyses of proteins important for cell-cycle regulation have shown that this organelle is used to sequester proteins, thereby inhibiting their activity.
References
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Journal ArticleDOI

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.
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