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Related Experiment Video

Updated: Apr 19, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A PP1-PP2A phosphatase relay controls mitotic progression.

Agnes Grallert1, Elvan Boke1, Anja Hagting2

  • 1Cell Division Group, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.

Nature
|December 10, 2014
PubMed
Summary
This summary is machine-generated.

A novel mitotic phosphatase relay involving protein phosphatase 1 (PP1) reactivates protein phosphatase 2A (PP2A) holoenzymes, coordinating cell division and exit in fission yeast. This conserved mechanism regulates PP2A-B55 and PP2A-B56 activities across eukaryotes.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cellular architecture undergoes significant reorganization during mitosis, primarily through protein phosphorylation.
  • Restoration of phosphatase activity is crucial for mitotic exit, with Cdc14 phosphatase in budding yeast and protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) in other eukaryotes implicated in this process.

Purpose of the Study:

  • To elucidate the mechanism of mitotic phosphatase regulation in fission yeast.
  • To identify the roles of PP1, PP2A-B55, and PP2A-B56 in coordinating mitotic progression and exit.

Main Methods:

  • Investigated the sequential activation of PP2A holoenzymes by PP1.
  • Analyzed the recruitment of PP1 (Dis2 isoform) to PP2A-B55 and PP2A-B56 regulatory subunits.
  • Examined the inhibition of PP1 by Cdk1-cyclin B and its subsequent auto-reactivation.

Main Results:

  • A mitotic phosphatase relay was identified where PP1 reactivation is essential for reactivating both PP2A-B55 and PP2A-B56.
  • PP1 is sequentially recruited to PP2A-B55 and PP2A-B56 holoenzymes, sequentially activating them.
  • PP1 activity is inhibited by Cdk1-cyclin B in early mitosis and reactivates as cyclin B levels decline, initiating the relay.

Conclusions:

  • PP1 reactivation initiates a cascade, first activating PP2A-B55, which then facilitates PP2A-B56 reactivation.
  • This conserved PP1-PP2A regulatory mechanism is vital for coordinating mitotic progression and exit in eukaryotes.
  • Conserved PP1-docking motifs suggest a broad role for PP1 in regulating PP2A activity in various signaling contexts.