Targets
Most information about the biochemical function of Cdc14 comes from studies of S. cerevisiae. In that species, one important target is Cdh1/Hct1. Cdh1 associates with the APC and leads to APC activity (anaphase promoting complex); activated APC is a key driver in mitotic exit. Furthermore, Cdc14 dephosphorylates the stoichiometric inhibitor of the mitotic cyclins, Sic1, stabilizing Sic1 protein. Cdc14 activity also leads to the stabilization of the transcription factor Swi5, leading to an upregulation of Sic1 transcription. It is possible that Cdc14 acts as a phosphatase on all Clb-Cdk1 targets, acting to reverse the effects of the mitotic cyclins.
The targets of Cdc14 are apparently quite diverse. Yeast two-hybrid and affinity capture methods have identified many proteins that potentially interact with ScCdc14, including those known to regulate the cell cycle and DNA replication, or that associate with the spindle or kinetochore. Cdc14 also appears to inhibit RNA polymerase I, which helps allow complete chromosome disjunction by eliminating ribosomal RNA (rRNA) transcripts that otherwise would block condensin binding to rDNA.
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