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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

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Published on: September 28, 2018

Structure and function of the PP2A-shugoshin interaction.

Zheng Xu¹, Bulent Cetin, Martin Anger

¹Department of Biological Structure, University of Washington, Seattle, WA 98195, USA.

|September 1, 2009

Summary

Shugoshin proteins (Sgo) protect chromosomes during cell division by binding to PP2A phosphatase. This interaction prevents cohesin loss, ensuring accurate segregation in meiosis I and supporting the spindle assembly checkpoint.

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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 18, 2009

Area of Science:

Cell Biology
Molecular Biology
Genetics

Background:

Accurate chromosome segregation is crucial for cell division, relying on shugoshin (Sgo) proteins to maintain cohesin at centromeres.
Shugoshin proteins interact with Protein Phosphatase 2A (PP2A) to regulate cohesin dephosphorylation, preventing its premature dissociation during meiosis I.

Purpose of the Study:

To elucidate the structural basis of the interaction between human Sgo1 and the PP2A holoenzyme.
To investigate the functional consequences of impaired Sgo-PP2A binding on chromosome segregation and the spindle assembly checkpoint.

Main Methods:

X-ray crystallography to determine the structure of the Sgo1-PP2A complex.
Biochemical assays to assess Sgo-PP2A binding and functional assays using mutant proteins in yeast and mammalian oocytes.

Main Results:

The crystal structure reveals that Sgo1 forms a homodimer that docks onto both the C and B' subunits of the AB'C PP2A holoenzyme.
Sgo1 homodimerization is essential for PP2A binding. Human Sgo1 (hSgo1) specifically binds AB'C PP2A, while Sgo2 interacts with all PP2A forms.
Mutants lacking PP2A-binding capability fail to protect centromeric cohesin during meiosis I and cannot support the spindle assembly checkpoint.

Conclusions:

Shugoshin-PP2A interaction is critical for maintaining cohesin integrity and ensuring accurate chromosome segregation.
Differential interactions of Sgo1 and Sgo2 with PP2A suggest distinct roles in regulating cellular processes.
Recruitment of PP2A to chromosomes is sufficient to protect cohesin from separase in mammalian oocytes, highlighting a conserved mechanism.