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Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...

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Related Experiment Video

Updated: May 27, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
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InterfERing with endoplasmic reticulum stress.

Honorata Kraskiewicz1, Una FitzGerald

  • 1National Centre for Biomedical Engineering Science, National University of Ireland, Galway, Ireland.

Trends in Pharmacological Sciences
|November 25, 2011
PubMed
Summary

Endoplasmic reticulum (ER) stress contributes to major diseases. Drugs targeting ER stress pathways show therapeutic potential, but further research is needed to understand their effects across all three arms.

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Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Endoplasmic reticulum (ER) stress is implicated in numerous diseases, including neurodegenerative disorders (Alzheimer's, Parkinson's), diabetes, cardiovascular disease, liver disorders, and cancer.
  • The therapeutic potential of drugs targeting ER stress pathways is significant due to its broad involvement in disease pathogenesis.

Purpose of the Study:

  • To review the effects of various drug classes on the three main arms of the ER stress response: PERK, ATF6, and IRE1.
  • To categorize drugs based on their mechanisms of action in modulating ER stress.

Main Methods:

  • Literature review of existing studies on drugs affecting ER stress.
  • Categorization of drugs into five groups: direct binders, chemical chaperones, protein degradation inhibitors, antioxidants, and calcium signaling modulators.

Main Results:

  • Drugs generally exhibit inhibitory effects on ER stress, leading to increased cellular viability, with notable exceptions in cancer cells.
  • The five drug categories demonstrate diverse mechanisms for interfering with ER stress signaling pathways.

Conclusions:

  • Targeting the ATF6 arm of ER stress warrants focused investigation.
  • Concurrent in vivo testing across all three ER stress arms (PERK, ATF6, IRE1) is crucial for fully realizing the therapeutic importance of modulating ER stress in human diseases.