Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit
2019
Sandra A. Touati | Lorena Hofbauer | Andrew W. Jones | Ambrosius P. Snijders | Gavin Kelly | Frank Uhlmann
Summary: Temporal control over protein phosphorylation and dephosphorylation is crucial for accurate chromosome segregation and for completion of the cell division cycle during exit from mitosis. In budding yeast, the Cdc14 phosphatase is thought to be a major regulator at this time, while in higher eukaryotes PP2A phosphatases take a dominant role. Here, we use time-resolved phosphoproteome analysis in budding yeast to evaluate the respective contributions of Cdc14, PP2ACdc55, and PP2ARts1. This reveals an overlapping requirement for all three phosphatases during mitotic progression. Our time-resolved phosphoproteome resource reveals how Cdc14 instructs the sequential pattern of phosphorylation changes, in part through preferential recognition of serine-based cyclin-dependent kinase (Cdk) substrates. PP2ACdc55 and PP2ARts1 in turn exhibit a broad substrate spectrum with some selectivity for phosphothreonines and a role for PP2ARts1 in sustaining Aurora kinase activity. These results illustrate synergy and coordination between phosphatases as they orchestrate phosphoproteome dynamics during mitotic progression. : By using time-resolved phosphoproteome analysis, Touati et al. illuminate the regulatory network that controls temporal order during chromosome segregation and cell division. The work highlights how three different phosphatases cooperate to shape phosphoproteome dynamics at this time, but each also makes unique contributions. Keywords: cell cycle, mitotic exit, phosphatases, Cdc14, PP2A, phosphoproteomics
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