During G2 phase of the cell cycle, Cdk1 and cyclin B1 makes a complex and forms maturation promoting factor (MPF). The complex accumulates in the nucleus due to phosphorylation of the cyclin B1 at multiple sites, which inhibits nuclear export of the complex.  Phosphorylation of Thr19 and Tyr15 residues of Cdk1 by Wee1 and MYT1 keeps the complex inactive and inhibits entry into mitosis whereas dephosphorylation of Cdk1 by CDC25C phosphatase at Thr19 and Tyr15 residues, activates the complex which is necessary in order to enter mitosis. Cdc25C phosphatase is present in the cytoplasm and in late G2 phase it is translocated into the nucleus by signaling such as PIK1, PIK3. The regulated translocation and accumulation of the multiple required signaling cascade components, MPF and its activator Cdc25, in the nucleus generates efficient activation of the MPF and produces switch-like, ultrasensitive entry into mitosis.
The figure shows different possible mechanisms for how increased regulation of the localization of signaling components by the stimulus (input signal) shifts the output from Michaelian response to ultrasensitive response. When stimulus is regulating only inhibition of Cdk1-cyclinB1 nuclear export, the outcome is Michaelian response, Fig (a). But if the stimulus can regulate localization of multiple components of the signaling cascade, i.e. inhibition of Cdk1-cyclinB1 nuclear export and translocation of the Cdc25C to nucleus, then the outcome is ultrasensitive response, Fig (b). As more components of the signaling cascade are regulated and localized by the stimulus—i.e. inhibition of Cdk1-cyclinB1 nuclear export, translocation of the Cdc25C to the nucleus, and activation of Cdc25C—the output response becomes more and more ultrasensitive, Fig(c).