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Regulating Secretory Proteostasis through the Unfolded Protein Response: From Function to Therapy

Lars Plate1, R Luke Wiseman1

  • 1Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.

Trends in Cell Biology
|June 26, 2017
PubMed

Insights

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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