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During M phase, Endosulfine (Endos) family proteins are phosphorylated byGreatwall kinase (Gwl), and the resultant pEndos inhibits the phosphatasePP2A-B55, which would otherwise prematurely reverse many CDK-drivenphosphorylations. We show here that PP2A-B55 is the enzyme responsible fordephosphorylating pEndos during M phase exit. The kinetic parameters forPP2A-B55's action on pEndos are orders of magnitude lower than those forCDK-phosphorylated substrates, suggesting a simple model for PP2A-B55regulation that we call inhibition by unfair competition. As the name suggests,during M phase PP2A-B55's attention is diverted to pEndos, which binds muchmore avidly and is dephosphorylated more slowly than other substrates. When Gwlis inactivated during the M phase-to-interphase transition, the dynamic balancechanges: pEndos dephosphorylated by PP2A-B55 cannot be replaced, so thephosphatase can refocus its attention on CDK-phosphorylated substrates. Thismechanism explains simultaneously how PP2A-B55 and Gwl together regulatepEndos, and how pEndos controls PP2A-B55.

Greatwall-phosphorylated Endosulfine is Both an Inhibitor and a Substrate of PP2A-B55 Heterotrimers