Zds1 regulates PP2ACdc55 activity and Cdc14 activation during mitotic exit via its Zds_C motif

Ines Calabria, Barbara Baro, Jose-Antonio Rodriguez-Rodriguez, Nuria Russi?ol and Ethel Queralt*

At anaphase onset, highly active mitotic cyclin-dependent kinase (Cdk) is inactivated to promote exit from mitosis and completion of cytokinesis. The budding yeast Cdc14p phosphatase is a key mitotic regulator that counteracts cyclin-dependent kinase (Cdk) activity during mitotic exit. Separase, together with Zds1p, promotes the down-regulation of PP2ACdc55 in early anaphase, enabling accumulation of phosphorylated forms of Net1p and nucleolar release of Cdc14p. Here we show that the C-terminal domain of Zds1p, called the Zds_C motif, is required for Zds1-induced release of Cdc14p, while the N-terminal domain of the protein might be involved in regulating this activity. More interestingly, Zds1p physically interacts with Cdc55p, and regulates its localization via the Zds_C motif. Nevertheless, expression of the Zds_C motif at endogenous levels cannot induce timely nucleolar release of Cdc14, despite the proper (nucleolar) localization of Cdc55p. Our results suggest that the activity of PP2ACdc55 cannot be modulated solely through regulation of its localization, and that an additional regulatory step may be required. These results suggest that Zds1p recruits PP2ACdc55 to the nucleolus and induces its inactivation by an unknown mechanism.

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