During sporulation, an atypical cytokinesis event occurs in which prospore membranes grow from the spindle pole bodies to engulf the meiotic nuclei. As the prospore membranes grow, they assume varying morphologies, first appearing as small cups, then forming elongated structures around the nucleus, before rounding up and closing. The leading edge of the growing prospore membrane is marked by a complex of proteins, which include Ssp1; these proteins are removed from the leading edge when the prospore membrane closes. We find that the GCKIII kinase encoded by SPS1 is required for this process, with SPS1 acting together with the sporulation-induced SPO77 to promote prospore membrane closure. Cells lacking either SPS1 or SPO77 make hyper-elongated prospore membranes that sometimes do not close. Previous studies show that cells lacking AMA1, which encodes an activator of the meiotic anaphase promoting complex, also have partially penetrant prospore membrane closure defects. Our genetic analyses demonstrate that SPS1 and SPO77 act in parallel to AMA1, as double mutants of either sps1 or spo77 and ama1 exhibit completely penetrant prospore membrane closure defects. We also find that SPS1 acts through SSP1. We see that Ssp1 is stabilized and not properly removed from the leading edge at the time of prospore membrane closure in sps1 mutants. Sps1 and Ssp1 are found in a complex, suggesting that the action of Sps1 on Ssp1 may be direct. Taken together, our results suggest that Sps1 regulates meiotic cytokinesis by promoting the proper degradation and/or removal of Ssp1. To determine how this cytokinetic event is coordinated with meiosis, we have examined how meiotic regulators interact with SPS1.