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Protein Phase Separation as a Stress Survival Strategy
Titus M Franzmann1, Simon Alberti1
1Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Cold Spring Harbor Perspectives in Biology
|January 9, 2019
Summary
Cells adapt to stress by forming protein condensates via phase separation. Prion-like domains act as sensors, regulating translation factors to promote survival in harsh conditions.
Area of Science:
- Cell biology
- Biochemistry
- Molecular biology
Background:
- Cells must adapt to environmental stress by altering physiology and metabolism.
- This adaptation involves down-regulating general gene expression and up-regulating protective factors like molecular chaperones.
Purpose of the Study:
- To investigate the role of phase separation in cellular stress adaptation.
- To explore how prion-like domains influence protein solubility and condensate formation under stress.
Main Methods:
- Review of recent findings on cellular stress response mechanisms.
- Analysis of the impact of physical-chemical parameters (temperature, pH) on protein solubility.
- Examination of the function of intrinsically disordered prion-like domains.
Main Results:
- Stress-induced changes in physical-chemical parameters alter the solubility of translation factors.
- These changes trigger phase separation, forming condensates that regulate translation factor activity.
- Prion-like domains function as environmentally regulated sensors modulating protein solubility and phase behavior.
Conclusions:
- Protein phase separation is a conserved mechanism cells use to adapt to stress.
- Condensate formation regulates cellular responses, enhancing fitness and survival.
- Prion-like domains are key regulators in stress-adaptive phase separation.
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