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Proteostasis In The Endoplasmic Reticulum: Road to Cure
Su Min Nam1,2, Young Joo Jeon1,2
1Department of Biochemistry, Chungnam National University College of Medicine, Daejeon 35015, Korea.
Cancers
|November 20, 2019
Summary
The unfolded protein response (UPR) in the endoplasmic reticulum (ER) manages protein homeostasis. Dysregulation of the UPR is linked to cancer, suggesting UPR-targeting therapies may improve cancer treatment outcomes.
Area of Science:
- Cellular Biology
- Molecular Biology
- Oncology
Background:
- The endoplasmic reticulum (ER) is vital for protein synthesis, folding, and trafficking, maintaining cellular proteostasis.
- Disruptions in ER folding capacity lead to ER stress, activating the unfolded protein response (UPR) to restore proteostasis.
- Persistent ER stress and UPR are implicated in cancer development, progression, and therapeutic resistance.
Purpose of the Study:
- To review recent advances in understanding the ER's UPR and its connection to mitochondria.
- To highlight the role of ER UPR in cancer pathogenesis and the tumor microenvironment.
- To discuss the potential of targeting ER UPR for cancer therapy.
Main Methods:
- Literature review of current research on ER stress and UPR in cancer.
- Analysis of the interplay between ER UPR and mitochondria.
- Exploration of therapeutic strategies targeting ER UPR.
Main Results:
- The UPR is a critical cellular response to ER stress, essential for maintaining proteostasis.
- ER stress and sustained UPR are significantly associated with various aspects of cancer, including tumor growth and immune evasion.
- The UPR influences the tumor microenvironment and is interconnected with mitochondrial function.
Conclusions:
- Targeting the ER UPR presents a promising therapeutic strategy for cancer treatment.
- Further research into UPR mechanisms and its targeting could lead to improved clinical outcomes in oncology.
- Understanding the ER-mitochondria UPR axis is crucial for developing novel cancer therapies.
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