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Updated: Aug 6, 2026
13:52
Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
Published on: July 9, 2013
The unfolded-protein-response pathway in yeast
1Department of Biochemistry and Biophysics, University of California Medical School, San Francisco, CA 94143-0448, USA.
Trends in Cell Biology
|February 1, 1994
Summary
The unfolded protein response (UPR) pathway, crucial for managing endoplasmic reticulum stress, involves a newly identified transmembrane kinase in yeast. This signaling system links the ER and nucleus in diverse organisms.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- The endoplasmic reticulum (ER) maintains protein homeostasis.
- Accumulation of unfolded proteins in the ER triggers adaptive responses.
- This signaling pathway is conserved across species, from yeast to mammals.
Purpose of the Study:
- To elucidate the molecular components of the unfolded-protein-response (UPR) pathway.
- To identify key regulators linking ER stress to nuclear responses.
- To characterize novel signaling molecules involved in ER stress management.
Main Methods:
- Investigated protein accumulation in the ER.
- Analyzed signaling pathways connecting the ER and nucleus.
- Utilized yeast as a model organism.
- Characterized a novel transmembrane kinase.
Main Results:
- Identified a transmembrane kinase as a critical component of the UPR pathway in yeast.
- Demonstrated the conserved nature of this ER-nucleus signaling system.
- Confirmed the kinase's structural similarity to growth-factor receptor kinases.
Conclusions:
- A transmembrane kinase is essential for the yeast unfolded-protein-response.
- This finding provides insights into conserved mechanisms of cellular stress response.
- The identified kinase represents a potential target for further research into ER-nucleus communication.
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