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How to design an optimal sensor network for the unfolded protein response
Wylie Stroberg1, Hadar Aktin2, Yonatan Savir2
1Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109-5622.
Molecular Biology of the Cell
|September 27, 2018
Summary
Chaperone-mediated sensors are more efficient than direct unfolded protein sensors for maintaining cellular protein homeostasis. This finding aids in designing optimal stress-sensing mechanisms for endoplasmic reticulum (ER) stress response.
Area of Science:
- Cellular Biology
- Biochemistry
- Systems Biology
Background:
- Cellular protein homeostasis relies on endoplasmic reticulum (ER) stress monitoring.
- Stress-detection networks modulate chaperone production to mitigate protein aggregation and misfolding.
Purpose of the Study:
- To model the unfolded protein response (UPR) in yeast.
- To optimize UPR sensing and activation strategies for balancing unfolded protein levels and chaperone production.
Main Methods:
- Developed a coarse model of the yeast UPR.
- Employed multi-objective optimization techniques.
- Compared direct unfolded protein sensing versus chaperone-mediated sensing.
Main Results:
- Chaperone-mediated sensors demonstrate superior efficiency over direct unfolded protein sensors.
- Separate activation and deactivation thresholds enhance chaperone-mediated sensor performance.
- Combined unfolded protein and unbound chaperone sensing offers no additional homeostatic advantage.
Conclusions:
- Chaperone-mediated sensing represents an optimized strategy for ER stress response.
- Findings provide insights for designing novel stress sensors.
- Suggests an evolutionary basis for BiP-regulated ER stress-sensing networks.
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