Progression of the mitotic cell cycle is driven by fluctuations of the cyclin-dependent kinase (Cdk) activities. Entry into mitosis is promoted by the elevated activity of Cdk1 associated with B-type cyclins. Conversely, exit from mitosis requires the inactivation of Cdk1 and the dephosphorylation of at least a subset of Cdk1 substrates. The Cdc14 family of phosphatases antagonizes the action of Cdk1, and is thus a major player in controlling the mitotic exit. We review recent discoveries in several model systems that have shed light on the function of Cdc14 and propose a general framework within which Cdc14 plays conserved roles in regulating the exit from mitosis and cytokinesis.