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Open AccessJournal ArticleDOI

Mitotic Exit in the Absence of Separase Activity

Ying Lu, +1 more
- 01 Mar 2009 - 
- Vol. 20, Iss: 5, pp 1576-1591
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TLDR
The first quantitative measure for Cdc14 release based on colocalization with the Net1 nucleolar anchor is defined, indicating efficient CDC14 release upon MEN activation; release driven by Esp1 in the absence of microtubules was inefficient and incapable of driving ME.
Abstract
In budding yeast, three interdigitated pathways regulate mitotic exit (ME): mitotic cyclin–cyclin-dependent kinase (Cdk) inactivation; the Cdc14 early anaphase release (FEAR) network, including a n...

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Citations
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Journal ArticleDOI

Phosphatases: providing safe passage through mitotic exit

TL;DR: This work has shown that the key mitotic exit phosphatase in budding yeast, Cdc14, is now well understood, and in animal cells, it is now emerging that mitoticexit relies on distinct regulatory networks, including the protein phosphatases PP1 and PP2A.
Journal ArticleDOI

Periodic cyclin-Cdk activity entrains an autonomous Cdc14 release oscillator.

TL;DR: An intrinsically oscillatory module controlling nucleolar release and resequestration of the Cdc14 phosphatase is demonstrated, which is essential for mitotic exit in budding yeast and suggests that the intrinsically autonomous CDC14 release cycles are locked at once-per-cell-cycle through entrainment by the Cdk oscillator in wild-type cells.
Journal ArticleDOI

Inhibition of Cdc42 during mitotic exit is required for cytokinesis

TL;DR: A decrease in Cdc42 activation during mitotic exit is necessary to allow localization of key cytokinesis regulators and proper septum formation.
Journal ArticleDOI

Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic processes.

TL;DR: The findings suggest the dephosphorylation of the formins may be important for their observed localization change during exit from mitosis and indicate that Cdc14 targets proteins involved in wide-ranging mitotic events.
Journal ArticleDOI

From START to FINISH: computational analysis of cell cycle control in budding yeast.

TL;DR: This work crafted a new mathematical model of cell cycle progression in yeast that exploits a natural separation of time scales in the cell cycle control network to construct a system of differential-algebraic equations for protein synthesis and degradation, post-translational modifications, and rapid formation and dissociation of multimeric complexes.
References
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Journal ArticleDOI

The dynamics of chromosome movement in the budding yeast Saccharomyces cerevisiae.

TL;DR: Nuclear DNA movement in the yeast was analyzed in live cells using digital imaging microscopy and corroborated by the analysis of nuclear DNA position in fixed cells to suggest that the mechanism of anaphase movement may be highly conserved.
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The SIN Kinase Sid2 Regulates Cytoplasmic Retention of the S. pombe Cdc14-like Phosphatase Clp1

TL;DR: It is shown that the most downstream SIN component, the Ndr-family kinase Sid2, maintains Clp1 in the cytoplasm in late mitosis by phosphorylating Clp 1 directly and thereby creating binding sites for the 14-3-3 protein Rad24.
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Red fluorescent protein (DsRed) as a reporter in Saccharomyces cerevisiae.

TL;DR: The utilization of a red fluorescent protein (DsRed) as an in vivo marker for Saccharomyces cerevisiae is described and a series of vectors are now available which can be used to create amino-terminal and carboxyl- terminal fusions with the DsRed protein.
Journal ArticleDOI

A Role for the FEAR Pathway in Nuclear Positioning during Anaphase

TL;DR: It is proposed that at anaphase onset, the FEAR pathway activates cytoplasmic microtubule-associated forces that facilitate chromosome segregation to the mother cell.
Journal ArticleDOI

Mitotic CDKs control the metaphase-anaphase transition and trigger spindle elongation.

TL;DR: It is shown that Clb-CDKs are important for the activation of the ubiquitin ligase Anaphase-Promoting Complex/Cyclosome (APC/C)-Cdc20 that triggers the metaphase-anaphase transition and anaphase spindle elongation.
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