Smk1 is a meiosis-specific MAPK that controls spore morphogenesis in S. cerevisiae. While Smk1 is activated by phosphorylation of its T-X-Y activation loop similar to other MAPKs, this pathway does not require a MAPK kinase family member. Instead, the CDK activating kinase, Cak1, phosphorylates Smk1 on the T, producing a low activity form of the enzyme that is uniformly distributed throughout the cell early in meiosis. Smk1 autophosphorylates the Y in-cis at prospore membranes (PSMs) at anaphase II. This spatiotemporally-regulated autophosphorylation reaction is triggered by Ssp2, a PSM-localized protein whose translation is induced specifically at anaphase II. To interrogate the mechanism of this developmentally-regulated autophosphorylation reaction, Smk1 activation has been reconstituted in bacterial cells and with purified proteins. Our data indicate that Ssp2 binding to Smk1 is sufficient to trigger Smk1 autophosphorylation. We previously reported that the meiosis-specific bridging protein for the anaphase promoting complex (Cdc20 homolog), Ama1, regulates Smk1 activation. We find that Ama1 controls Smk1 autophosphorylation by influencing the interaction of Smk1 and Ssp2 at the PSM. Thus, despite the timely production and localization of Smk1 and Ssp2 to PSMs in the ama1∆ background, they fail to form a complex. We will present a model in which Ama1 triggers the productive interaction of Ssp2 and Smk1, thereby coupling the completion of the meiotic chromosome cycle to spore wall differentiation.