Orchestrating anaphase and mitotic exit: separase cleavage and localization of Slk19

Lehane, Christine M.; Uhlmann, Frank

doi:10.1038/ncb0901-771

Cited by 137 publications

(151 citation statements)

References 35 publications

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“…Although deletion of either SLK19 or SPO12 resulted in broken and short spindles in cdc15-2 background, cdc15-2 slk19⌬ cells showed more severe broken spindle phenotype, presumably due to the direct role of Slk19 in spindle stability (Fig. 5 C and D) (19,21). These observations suggest that FEAR may facilitate spindle elongation by antagonizing Clb5-Cdk1 function.…”

Section: Fear-induced Cdc14 Release Is Required For Anaphase Progressmentioning

confidence: 64%

Temporal control of the dephosphorylation of Cdk substrates by mitotic exit pathways in budding yeast

Jin

Liu²,

Liang³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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The temporal phosphorylation of cell cycle-related proteins by cyclin-dependent kinases (Cdks) is critical for the correct order of cell cycle events. In budding yeast, CDC28 encodes the only Cdk and its association with various cyclins governs the temporal phosphorylation of Cdk substrates. S-phase Cdk substrates are phosphorylated earlier than mitotic Cdk substrates, which ensures the sequential order of DNA synthesis and mitosis. However, it remains unclear whether Cdk substrates are dephosphorylated in temporally distinct windows. Cdc14 is a conserved protein phosphatase responsible for the dephosphorylation of Cdk substrates. In budding yeast, FEAR (Cdc14 early anaphase release) and MEN (mitotic exit network) activate phosphatase Cdc14 by promoting its release from the nucleolus in early and late anaphase, respectively. Here, we show that the sequential Cdc14 release and the distinct degradation timing of different cyclins provides the molecular basis for the differential dephosphorylation windows of S-phase and mitotic cyclin substrates. Our data also indicate that FEAR-induced dephosphorylation of S-phase Cdk substrates facilitates anaphase progression, revealing an extra layer of mitotic regulation.Cdc14 phosphatase ͉ spindle ͉ Clb5 ͉ Clb2 ͉ anaphase

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Section: Fear-induced Cdc14 Release Is Required For Anaphase Progressmentioning

confidence: 64%

Temporal control of the dephosphorylation of Cdk substrates by mitotic exit pathways in budding yeast

Jin

Liu²,

Liang³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…Since Cdc5 plays a role in both the FEAR and the MEN (see below), Cdc5 may coordinate these two pathways, perhaps by directly phosphorylating and regulating components in each pathway. Interestingly, Slk19 cleavage by Esp1 is shown to require its phosphorylation (Sullivan et al, 2001). Since Scc1 cleavage by Esp1 is promoted by Cdc5-dependent phosphorylation, it will be interesting to examine whether Cdc5 phosphorylates Slk19 to promote its cleavage.…”

Section: Fear and Mitotic Exitmentioning

confidence: 99%

“…In addition, catalytic activity of Esp1 and cleavage of its kinetochore-associating substrate Slk19 (Zeng et al, 1999) are not required for the FEAR (Sullivan and Uhlmann, 2003). Rather, this activity appears to be important for the function of late mitotic spindles, since the Esp1-cleaved Slk19 C-terminal fragment localizes and stabilizes the anaphase spindle (Sullivan et al, 2001). At present, how the FEAR pathway is activated and how the signal for the Cdc14 release is relayed is not known.…”

Section: Fear and Mitotic Exitmentioning

confidence: 99%

Yeast polo-like kinases: functionally conserved multitask mitotic regulators

et al. 2005

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The polo-like kinases (Plks) are a conserved subfamily of Ser/Thr protein kinases that play pivotal roles in regulating various cellular and biochemical events at multiple stages of M phase. Genetic and biochemical data revealed that both the budding yeast and the fission yeast polo kinase homologs (Cdc5 and Plo1, respectively) bear remarkable functional similarities with those in metazoan organisms, suggesting that the role of Plks is largely conserved throughout evolution. Thus, studies on Plks in genetically amenable lower eucaryotic organisms may yield valuable insights into the function of Plks in higher eucaryotic organisms. In this review, common properties and distinct functions of Cdc5 and Plo1 will be discussed and compared to properties and functions of Plks in higher eucaryotic organisms.

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“…However, remarkably, Esp1's protease activity seems not to be required for its mitotic exit function (Sullivan and Uhlmann, 2003). The FEAR network component Slk19 localizes to kinetochores and the spindle mid-zone during anaphase and is a substrate of Esp1 (Zeng et al, 1999;Sullivan et al, 2001). Spo12 encodes a protein of unknown function.…”

Section: Introductionmentioning

confidence: 99%

The Role of the Polo Kinase Cdc5 in Controlling Cdc14 Localization

Visintin

Stegmeier

Amon

2003

MBoC

119

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In budding yeast, the protein phosphatase Cdc14 controls exit from mitosis. Its activity is regulated by a competitive inhibitor Cfi1/Net1, which binds to and sequesters Cdc14 in the nucleolus. During anaphase, Cdc14 is released from its inhibitor by the action of two regulatory networks. The Cdc Fourteen Early Anaphase Release (FEAR) network initiates Cdc14 release from Cfi1/Net1 during early anaphase, and the Mitotic Exit Network (MEN) promotes Cdc14 release during late anaphase. Here, we investigate the relationship among FEAR network components and propose an order in which they function to promote Cdc14 release from the nucleolus. Furthermore, we examine the role of the protein kinase Cdc5, which is a component of both the FEAR network and the MEN, in Cdc14 release from the nucleolus. We find that overexpression of CDC5 led to Cdc14 release from the nucleolus in S phase-arrested cells, which correlated with the appearance of phosphorylated forms of Cdc14 and Cfi1/Net1. Cdc5 promotes Cdc14 phosphorylation and, by stimulating the MEN, Cfi1/Net1 phosphorylation. Furthermore, we suggest that Cdc14 release from the nucleolus only occurs when Cdc14 and Cfi1/Net1 are both phosphorylated.

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Orchestrating anaphase and mitotic exit: separase cleavage and localization of Slk19

Cited by 137 publications

References 35 publications

Temporal control of the dephosphorylation of Cdk substrates by mitotic exit pathways in budding yeast

Temporal control of the dephosphorylation of Cdk substrates by mitotic exit pathways in budding yeast

Yeast polo-like kinases: functionally conserved multitask mitotic regulators

The Role of the Polo Kinase Cdc5 in Controlling Cdc14 Localization

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