Suppression of Scant Identifies Endos as a Substrate of Greatwall Kinase and a Negative Regulator of Protein Phosphatase 2A in Mitosis
2011

Greatwall Kinase and Endos Regulate Protein Phosphatase 2A in Mitosis

publication Evidence: high

Author Information

Author(s): Rangone Hélène, Wegel Eva, Gatt Melanie K., Yeung Eirene, Flowers Alexander, Debski Janusz, Dadlez Michal, Janssens Veerle, Carpenter Adelaide T. C., Glover David M.

Primary Institution: Department of Genetics, University of Cambridge, Cambridge, United Kingdom

Hypothesis

How does Greatwall kinase regulate the activity of Protein Phosphatase 2A during mitosis?

Conclusion

Greatwall kinase and Endos work together to inhibit Protein Phosphatase 2A, which is crucial for proper mitotic progression.

Supporting Evidence

  • Mutations in the regulatory subunit of PP2A enhance the effects of Greatwall mutations.
  • Endos acts as a suppressor of the dominant gwlScant phenotype.
  • Greatwall phosphorylates Endos at a specific site essential for its function.
  • Endos depletion leads to mitotic defects similar to those observed in gwl mutants.
  • PP2A is a major phosphatase that dephosphorylates Cdk1 substrates during mitosis.

Takeaway

This study shows that two proteins, Greatwall and Endos, help control a process that allows cells to divide properly by managing another protein that removes signals needed for division.

Methodology

The researchers used genetic mutations in Drosophila to study the interactions between Greatwall kinase, Endos, and Protein Phosphatase 2A.

Digital Object Identifier (DOI)

10.1371/journal.pgen.1002225

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