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Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
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Stress granules display bistable dynamics modulated by Cdk.

Galal Yahya1,2, Alexis P Pérez1,3, Mònica B Mendoza1

  • 1Molecular Biology Institute of Barcelona, Spanish National Research Council, Catalonia, Spain.

The Journal of Cell Biology
|January 22, 2021
PubMed
Summary
This summary is machine-generated.

Stress granules (SGs) and Cdc28 kinase form a mutual-inhibition loop. Whi8 protein in SGs inhibits translation and Cdc28 activity, while also promoting SG dissolution, creating a bistable switch.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Stress granules (SGs) are essential biomolecular condensates formed under stress.
  • Their regulation and functional roles are not fully understood.
  • Cdc28 is a key cell cycle regulator in budding yeast.

Purpose of the Study:

  • To elucidate the regulatory interplay between SGs and Cdc28.
  • To identify novel regulators of SG dynamics and function.
  • To investigate the role of RNA-binding proteins in SG regulation.

Main Methods:

  • Yeast genetics and molecular biology techniques.
  • Biochemical assays to study protein-protein and protein-RNA interactions.
  • Microscopy to visualize SG dynamics and localization.

Main Results:

  • Identified Whi8, an RNA-binding protein, as a key component of SGs.
  • Demonstrated Whi8's dual role in inhibiting CLN3 translation and recruiting Cdc28 to SGs.
  • Uncovered a mutual-inhibition mechanism between SGs and Cdc28, forming a bistable system.
  • Showed that Whi8 promotes SG dissolution by recruiting Cdc28.

Conclusions:

  • A novel mutual-inhibition circuit between SGs and Cdc28 governs SG dynamics.
  • Whi8 acts as a crucial link, modulating translation and SG stability.
  • This SG-Cdc28 bistable switch is conserved in mammalian cells, suggesting a fundamental regulatory mechanism.