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Updated: May 21, 2025
09:57
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
Published on: December 17, 2016
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Proteasome condensates repeatedly "contact and release" at the nuclear periphery during dissolution
Conner Butcher1, Kyle VanderVen1, Jianhui Li1
1Biomedical Engineering and Science, Florida Institute of Technology, Melbourne, Florida, United States.
Micropublication Biology
|March 20, 2025
Summary
Stress causes proteasome condensates to form in yeast. Upon glucose recovery, these condensates rapidly dissolve, with proteasomes returning to the nucleus via membrane interactions.
Area of Science:
- Cell Biology
- Biochemistry
Background:
- Stress-induced proteasome condensates are observed in yeast and mammalian cells.
- Proteasome condensate properties and dynamics are stress-dependent.
- In *Saccharomyces cerevisiae*, cytoplasmic proteasome condensates form from nuclear proteasomes during glucose starvation.
Purpose of the Study:
- To characterize the kinetics and dynamics of proteasome condensate dissolution after glucose recovery.
- To investigate the mechanisms underlying biomolecular condensate dissolution.
Main Methods:
- Observation of proteasome condensate behavior in *Saccharomyces cerevisiae*.
- Analysis of proteasome condensate dynamics during glucose recovery.
- Characterization of proteasome reimport into the nucleus.
Main Results:
- Proteasome condensates dissipate rapidly upon glucose recovery.
- Proteasomes reimport to the nucleus within minutes after glucose restoration.
- Dissolving proteasome condensates exhibit transient association with nuclear membranes through "contact and release" movements.
Conclusions:
- The study elucidates the dynamic process of proteasome condensate dissolution.
- Transient nuclear membrane association is a key feature of proteasome condensate disassembly.
- Provides novel insights into the mechanisms governing biomolecular condensate dissolution.
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