Abstract
During G1 in budding yeast, the Cdc42 GTPase establishes a polar front, along which actin is recruited to direct secretion for bud formation. Cdc42 localizes at the bud cortex and then redistributes between mother and daughter in anaphase. The molecular mechanisms that terminate Cdc42 bud-localized activity during mitosis are poorly understood. We demonstrate that the activity of the Cdc14 phosphatase, released through the mitotic exit network, is required for Cdc42 redistribution between mother and bud. Induced Cdc14 nucleolar release results in premature Cdc42 redistribution between mother and bud. Inhibition of Cdc14 causes persistence of Cdc42 bud localization, which perturbs normal cell size and spindle positioning. Bem3, a Cdc42 GAP, binds Cdc14 and is dephosphorylated at late anaphase in a Cdc14-dependent manner. We propose that Cdc14 dephosphorylates and activates Bem3 to allow Cdc42 inactivation and redistribution. Our results uncover a mechanism through which Cdc14 regulates the spatiotemporal activity of Cdc42 to maintain normal cell size at cytokinesis.