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Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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The Unfolded Protein Response01:37

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Hormones intricately bind to receptors on the surface or within target cells, initiating a cascade of cellular responses.
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The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
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Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
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Endoplasmic Reticulum Stress Modulates Therapeutic Responses in Hepatocellular Carcinoma.

Yi-Li Chen1, Chen-Wei Chou1, I-Hsiu Liu1

  • 1Department of Cell Biology and Anatomy, College of Medicine, National Cheng Kung University, Tainan, Taiwan.

Chemotherapy
|August 4, 2025
PubMed
Summary

The unfolded protein response (UPR) helps liver cancer cells survive chemotherapy by activating survival pathways. Targeting UPR and ER stress may offer new therapeutic strategies for hepatocellular carcinoma (HCC).

Keywords:
Endoplasmic reticulum stressHepatocellular carcinomaUnfolded protein response

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Area of Science:

  • Oncology
  • Molecular Biology
  • Cellular Stress Response

Background:

  • Hepatocellular carcinoma (HCC) mortality is rising, with chemotherapy and targeted therapies being primary treatments.
  • Prolonged treatment for HCC can lead to drug resistance and recurrence, impacting patient outcomes.
  • The unfolded protein response (UPR) is a cellular stress mechanism that can promote cancer cell survival and drug resistance.

Purpose of the Study:

  • To review genetic molecules and signaling pathways regulated by the UPR in liver cancer.
  • To investigate the influence of UPR-regulated pathways on the effectiveness of HCC drugs.
  • To summarize the roles of UPR-induced lipid droplet formation and inflammation in HCC development and drug resistance.

Main Methods:

  • Literature review of studies on UPR, ER stress, and their role in HCC.
  • Analysis of genetic molecules and signaling pathways influenced by UPR.
  • Examination of UPR's impact on cellular processes like DNA repair, autophagy, and apoptosis in HCC.

Main Results:

  • UPR activation is crucial for HCC cell growth and survival under drug-induced stress.
  • UPR-regulated pathways contribute to cancer cell resistance against chemotherapy and targeted therapies.
  • Lipid droplet formation and inflammatory stimulation are partial effects of UPR involved in HCC progression.

Conclusions:

  • Understanding UPR-mediated mechanisms is key to overcoming drug resistance in HCC.
  • Targeting the endoplasmic reticulum (ER) stress pathways offers a promising therapeutic avenue for HCC.
  • Interfering with UPR signaling could enhance the efficacy of current HCC treatments.