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Regulating Secretory Proteostasis through the Unfolded Protein Response: From Function to Therapy
1Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
Trends in Cell Biology
|June 26, 2017
Summary
Disruptions in secretory proteostasis cause protein misfolding diseases. Targeting the endoplasmic reticulum unfolded protein response (UPR) may offer therapeutic strategies for these conditions.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- Secretory proteostasis imbalances are linked to protein misfolding diseases.
- Organisms possess stress-responsive pathways, like the endoplasmic reticulum (ER) unfolded protein response (UPR), to maintain proteostasis.
- UPR signaling is crucial for managing ER stress and protecting the secretory proteome.
Purpose of the Study:
- To elucidate how UPR activation impacts ER and downstream secretory proteostasis.
- To explore the therapeutic potential of targeting UPR pathways for protein misfolding diseases.
Main Methods:
- Review of recent scientific literature on UPR signaling and proteostasis.
- Analysis of studies investigating the effects of UPR activation on secretory environments.
- Examination of evidence for therapeutic interventions targeting UPR pathways.
Main Results:
- Recent reports define how specific UPR pathways influence proteostasis within the ER and beyond.
- Evidence suggests UPR activation plays a significant role in maintaining secretory proteostasis under stress.
Conclusions:
- Understanding UPR's impact on proteostasis is key to developing new treatments.
- Targeting UPR signaling presents a promising therapeutic avenue for diverse protein misfolding diseases.
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