In Saccharomyces cerevisiae exit from mitosis requires the Cdc14 phosphatase to reverse CDK-mediated phosphorylation. Cdc14 is released from the nucleolus by the Cdc14 early anaphase release (FEAR) and mitotic exit network (MEN) pathways. In meiosis, the FEAR pathway is essential for exit from anaphase I. The MEN component Cdc15 is required for the formation of mature spores. To analyze the role of Cdc15 during sporulation, a conditional mutant in which CDC15 expression was controlled by the CLB2 promoter was used. Cdc15-depleted cells proceeded normally through the meiotic divisions but were unable to properly disassemble meiosis II spindles. The morphology of the prospore membrane was aberrant and failed to capture the nuclear lobes. Cdc15 was not required for Cdc14 release from the nucleoli, but it was essential to maintain Cdc14 released and for its nucleo-cytoplasmic transport. However, cells carrying a CDC14 allele with defects in nuclear export (Cdc14-DNES) were able to disassemble the spindle and to complete spore formation, suggesting that the Cdc14 nuclear export defect was not the cause of the phenotypes observed in cdc15 mutants.
MEIOSIS is a specialized cell division that produces the haploid cells needed for sexual reproduction, and the completion of meiosis is normally coupled to differentiation programs that produce gametes. In Saccharomyces cerevisiae, sporulation is initiated when diploid cells are grown in the absence of nitrogen and the presence of a nonfermentable carbon source such as acetate (Esposito and Klapholtz 1981). When triggered to enter the sporulation program, cells exit the mitotic cycle from the G1 phase. This is followed by one round of S phase and two meiotic divisions that generate four haploid nuclei, which are packaged into individual spores. As a consequence of this process, four haploid gametes (spores) are formed in the cytoplasm of the mother cell (ascus) (reviewed by Neiman 2005). At the onset of meiosis II, the spindle pole body (SPB) is modified by the incorporation of several meiosis-specific proteins, which together make up the meiosis II outer plaque (Knop and Strasser 2000;Bajgier et al. 2001;Nickas et al. 2003). This change in composition converts the function of the cytoplasmic face of the SPB from microtubule nucleation to membrane nucleation. The process of spore construction requires the de novo assembly of two cellular structures, the prospore membrane (PSM) that is generated around the daughter nuclei to create prospores and a protective spore wall that surrounds the prospores. Once the meiosis II outer plaque of the SPB has been assembled, it becomes a site for the docking and coalescence of secretory vesicles to form flattened double-membrane sheets termed PSMs (Moens 1971;Neiman 1998). These nascent PSMs expand during meiosis II, and at the time of nuclear division each PSM completely engulfs the nuclear lobe to which it is anchored via the SPB. At the completion of meiosis II, each PSM fuses with itself so that each daughter nucleus (and assoc...