Dual control of mitotic exit

Article Abstract:

It has been established that the protein Cdc20 has a dual role in prompting the final cell cycle transition, exit from mitosis. Cdc20 facilitates the degradation of a protein known as Pds1, thus releasing Cdc14 from where it is trapped in the nucleolus. Through inducing degradation of Clb5, an antagonist of Cdc14, Cdc20 allows Cdc14 to efficiently dephosphorylate its targets. This research has given a valuable insight into how Cdc20 regulates exit from mitosis. The next stage will be to establish how Cdc20's substrates control the activity of Cdc14.

Cell cycle

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APC(super Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5

Article Abstract:

It appears that proteolysis of the S phase cyclin Clb5 and Pds1 by the activating subunit Cdh1/Hct1 (APC(super Cdc20)) at the metaphase-to-anaphase transition mediates Cdk1 inactivation by two mechanisms. Proteolysis of Pds1 allows release of Cdc14 from the nucleolus, while proteolysis of Clb5 makes this phosphatase able to activate Sic1 and Cdh1. Cells lacking both Pds1 and Clb5 are able to proliferate in the total absence of Cdc20.

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Cfi1 prevents premature exit from mitosis by anchoring Cdc14 phosphatase in the nucleolus

Article Abstract:

Mitosis is induced by the activation of mitotic cyclin-dependent kinases (CDKs), and inactivation results in cells leaving mitosis. Cdc14 is shown to be sequestered in the nucleolus during most of the cycle cycle. It is released from the nucleolus during nuclear division, enabling it to reach its targets. This movement of Cdc14 during anaphase, requires a highly conserved signalling cascade.

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