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Related Experiment Video

Updated: Feb 12, 2026

High-resolution Imaging and Analysis of Individual Astral Microtubule Dynamics in Budding Yeast
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Phosphoproteome dynamics during mitotic exit in budding yeast.

Sandra A Touati1, Meghna Kataria1, Andrew W Jones2

  • 1Chromosome Segregation Laboratory, The Francis Crick Institute, London, UK.

The EMBO Journal
|April 14, 2018
PubMed
Summary

Mitotic exit involves ordered dephosphorylation and new phosphorylation events. Budding yeast studies reveal key roles for cyclin-dependent kinases (Cdks) and Polo kinase in regulating these dynamic phosphorylation changes during cell division.

Keywords:
cell cyclekinasesmitosisphosphatasesphosphoproteomics

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The cell division cycle concludes with mitosis, producing two daughter cells.
  • Mitotic progression involves precise regulation of protein phosphorylation and dephosphorylation.
  • Cyclin-dependent kinases (Cdks) and the anaphase-promoting complex/cyclosome (APC/C) are central regulators of mitosis.

Purpose of the Study:

  • To analyze phosphorylation dynamics during mitotic exit in budding yeast.
  • To identify the kinases and phosphatases involved in ordering dephosphorylation events.
  • To investigate the role of new phosphorylation events during mitotic exit.

Main Methods:

  • High-resolution temporal analysis of 3,456 phosphosites on 1,101 proteins.
  • Synchronous progression of budding yeast cells through mitosis.
  • Quantitative phosphoproteomics.

Main Results:

  • Ordered dephosphorylation events are orchestrated by the successive inactivation of S and M phase Cdks and Polo kinase.
  • A significant number of new phosphorylation events occur concurrently with dephosphorylation.
  • These new phosphorylations correlate with late mitotic kinase activation, identifying novel kinase targets.

Conclusions:

  • Mitotic exit is a dynamic process involving both dephosphorylation and phosphorylation.
  • Multiple mitotic kinases contribute to the precise ordering of these phosphorylation events.
  • The study revises the understanding of mitotic exit regulation.