Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit
Abstract
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, PP2A Cdc55 , and PP2A Rts1 . 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. PP2A Cdc55 and PP2A Rts1 in turn exhibit a broad substrate spectrum with some selectivity for phosphothreonines and a role for PP2A Rts1 in sustaining Aurora kinase activity. These results illustrate synergy and coordination between phosphatases as they orchestrate phosphoproteome dynamics during mitotic progression.
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BibTeX
@article{touati2026cdc14,
title = {{Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit}},
author = {Sandra Touati and Lorena Hofbauer and Andrew Jones and Ambrosius Snijders and Gavin Kelly and Frank Uhlmann},
journal = {Cell Reports},
year = {2026},
month = sep,
doi = {10.1016/j.celrep.2019.10.041},
url = {https://hal.science/hal-05750142v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit
AU - Sandra Touati
AU - Lorena Hofbauer
AU - Andrew Jones
AU - Ambrosius Snijders
AU - Gavin Kelly
AU - Frank Uhlmann
PY - 2026
DA - 2026/09/15
JO - Cell Reports
DO - 10.1016/j.celrep.2019.10.041
UR - https://hal.science/hal-05750142v1
AB - 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, PP2A Cdc55 , and PP2A Rts1 . 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. PP2A Cdc55 and PP2A Rts1 in turn exhibit a broad substrate spectrum with some selectivity for phosphothreonines and a role for PP2A Rts1 in sustaining Aurora kinase activity. These results illustrate synergy and coordination between phosphatases as they orchestrate phosphoproteome dynamics during mitotic progression.
SN - 2211-1247
SN - 2211-1247
ER -