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Vol. 20, Issue 1, 134-145, January 1, 2009
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*Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215; and
Laboratory of Biological Chemistry, Graduate School of Agricultural and Life Science, The University of Tokyo, Tokyo 113-8657, Japan
Submitted June 18, 2008;
Revised October 6, 2008;
Accepted October 9, 2008
Monitoring Editor: Mark J. Solomon
Ascospore formation in yeast is accomplished through a cell division in which daughter nuclei are engulfed by newly formed plasma membranes, termed prospore membranes. Closure of the prospore membrane must be coordinated with the end of meiosis II to ensure proper cell division. AMA1 encodes a meiosis-specific activator of the anaphase promoting complex (APC). The activity of APCAma1 is inhibited before meiosis II, but the substrates specifically targeted for degradation by Ama1 at the end of meiosis are unknown. We show here that ama1
mutants are defective in prospore membrane closure. Ssp1, a protein found at the leading edge of the prospore membrane, is stabilized in ama1
mutants. Inactivation of a conditional form of Ssp1 can partially rescue the sporulation defect of the ama1
mutant, indicating that an essential function of Ama1 is to lead to the removal of Ssp1. Depletion of Cdc15 causes a defect in meiotic exit. We find that prospore membrane closure is also defective in Cdc15 and that this defect can be overcome by expression of a form of Ama1 in which multiple consensus cyclin-dependent kinase phosphorylation sites have been mutated. These results demonstrate that APCAma1 functions to coordinate the exit from meiosis II with cytokinesis.
Address correspondence to: Aaron M. Neiman (aaron.neiman{at}sunysb.edu)
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