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Endoplasmic reticulum stress response in yeast and humans
Haoxi Wu, Benjamin S H Ng1, Guillaume Thibault
1*School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.
Bioscience Reports
|June 10, 2014
Summary
The unfolded protein response (UPR) pathway maintains endoplasmic reticulum (ER) homeostasis. This review details UPR mechanisms across yeast and humans, highlighting its role in disease.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- The unfolded protein response (UPR) is a critical intracellular signaling pathway that monitors endoplasmic reticulum (ER) homeostasis.
- UPR activation is essential for mitigating ER stress, a conserved process across eukaryotes from yeast to humans.
- While metazoans possess three UPR outputs, yeast exclusively utilize the inositol-requiring enzyme-1 (Ire1) pathway.
Purpose of the Study:
- To review major advancements in understanding ER stress response mechanisms.
- To discuss the role of protein structures in elucidating UPR pathways.
- To explore the connection between ER stress and disease development.
Main Methods:
- Comparative analysis of UPR pathways in Saccharomyces cerevisiae, Schizosaccharomyces pombe, and humans.
- Review of literature on protein structure contributions to UPR understanding.
- Synthesis of current knowledge on ER stress and its implication in diseases.
Main Results:
- The UPR pathway activates hundreds of genes to restore ER homeostasis, but failure can lead to apoptosis.
- The Ire1 pathway is a conserved and fundamental component of the UPR in eukaryotes.
- Structural biology provides key insights into the molecular mechanisms of UPR signaling.
Conclusions:
- Understanding ER stress and UPR is crucial for comprehending cellular health and disease.
- The conserved nature of UPR highlights its fundamental importance in cellular stress management.
- Further research into UPR mechanisms, aided by structural data, may reveal new therapeutic targets for ER-related diseases.
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