Format

Send to

Choose Destination
Cell Rep. 2019 Nov 12;29(7):2105-2119.e4. doi: 10.1016/j.celrep.2019.10.041.

Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit.

Author information

1
Chromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK. Electronic address: sandra.touati@sorbonne-universite.fr.
2
Chromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
3
Mass Spectrometry Proteomics Science Technology Platform, The Francis Crick Institute, London NW1 1AT, UK.
4
Bioinformatics & Biostatistics Science Technology Platform, The Francis Crick Institute, London NW1 1AT, UK.
5
Chromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK. Electronic address: frank.uhlmann@crick.ac.uk.

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, 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.

KEYWORDS:

Cdc14; PP2A; cell cycle; mitotic exit; phosphatases; phosphoproteomics

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center