The fundamental mechanisms of mitosis are conserved throughout evolution in eukaryotes, including ubiquitin-mediated proteolysis of cell-cycle regulators by the anaphase promoting complex/cyclosome (APC). The spindle checkpoint protein Cdc20 activates the APC in a substrate-specific manner. It is present in the cytoplasm and concentrated in the centrosomes throughout the cell cycle, accumulates at the kinetochores in metaphase, and is no longer detected following anaphase. However, it is unknown if Cdc20 has the same activities and distribution during meiosis in male germ cells. We found that in mice Cdc20 accumulates in the cytoplasm of pachytene spermatocytes during meiosis I, is distributed throughout spermatocytes undergoing meiotic division, and is present in the cytoplasm of post-meiotic spermatids. Several proteins bind to and regulate the function of Cdc20 during mitosis. We identified speriolin, determined that it is a novel spermatogenic cell-specific Cdc20-binding protein, is present in the cytoplasm and is concentrated at the centrosomes of spermatocytes and spermatids, and that a leucine zipper domain is required to target speriolin to the centrosome. The seven tandem WD motifs of Cdc20 probably fold into a seven-blade beta-propeller structure, and we determined that they are required for speriolin binding and for localization of Cdc20 to the centrosomes and nucleus, suggesting that speriolin might regulate or stabilize the folding of Cdc20 during meiosis in spermatogenic cells.