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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Cdc14 and the temporal coordination between mitotic exit and chromosome segregation.
TL;DR: This work has shown that cohesin cleavage alone is not sufficient for the segregation of the entire genome and that repetitive regions, such as the ribosomal DNA array and telomeres, require additional mechanisms during mitotic disjunction.
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Cyclin B1-Cdk1 facilitates MAD1 release from the nuclear pore to ensure a robust spindle checkpoint
Mark Jackman,Chiara Marcozzi,Martina Barbiero,Mercedes Pardo,Lu Yu,Adam L. Tyson,Jyoti S. Choudhary,Jonathon Pines +7 more
TL;DR: Cyclin B1-Cdk1, the major mitotic kinase, binds to the spindle checkpoint protein MAD1 and synergizes with MPS1 to facilitate MAD1 release from the nuclear pore complex and recruitment to kinetochores before nuclear envelope breakdown.
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Dephosphorylating eukaryotic RNA polymerase II
TL;DR: In this article, the specific roles of CTD phosphatases in regulating transcription are discussed and the specificity and timing of dephosphorylation are achieved for these proteins and various regulatory factors that affect these dynamics.
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A decade of Cdc14 – a personal perspective Delivered on 9 July 2007 at the 32nd FEBS Congress in Vienna, Austria
TL;DR: Findings are reviewed focusing on how discoveries in the laboratory helped elucidate the function and regulation of Cdc14, the key trigger of exit from mitosis in budding yeast.
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The p53-targeting human phosphatase hCdc14A interacts with the Cdk1/cyclin B complex and is differentially expressed in human cancers
Michelle T. Paulsen,Adrienne M Starks,Frederick A. Derheimer,Sheela Hanasoge,Liwu Li,Jack E. Dixon,Mats Ljungman +6 more
TL;DR: It is shown that hCdc14A is differentially expressed in human tissues and in 75 cancer cell lines examined and that it forms a complex with Cdk1/cyclin B during interphase but not during mitosis, implicate that dysregulation of hCDC14A expression may play a role in carcinogenesis.
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.