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Related Concept Videos

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...
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...
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...
Endoplasmic Reticulum01:39

Endoplasmic Reticulum

The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
Chronic Inflammation: Introduction01:12

Chronic Inflammation: Introduction

Chronic inflammation is a prolonged, dysregulated immune response that persists for weeks to years when the inciting stimulus is difficult to eradicate or when self‑antigens drive ongoing reactivity. Morphologically, it is defined by mononuclear cell infiltration, progressive tissue destruction, and concurrent attempts at healing via angiogenesis and fibrosis. Compared with acute inflammation, edema is less prominent while cellular infiltration predominates; triggers include persistent...

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Related Experiment Video

Updated: May 25, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

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

Published on: June 14, 2024

The interplay between endoplasmic reticulum stress and inflammation.

Sumaira Z Hasnain1, Rohan Lourie, Indrajit Das

  • 1Immunity, Infection and Inflammation Program, Mater Medical Research Institute, Mater Hospitals, South Brisbane, Queensland, Australia.

Immunology and Cell Biology
|January 18, 2012
PubMed
Summary

Endoplasmic reticulum (ER) stress triggers and results from chronic inflammation. This review explores how ER stress and the unfolded protein response (UPR) interact with inflammation in various diseases.

Related Experiment Videos

Last Updated: May 25, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

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

Published on: June 14, 2024

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Endoplasmic reticulum (ER) stress is implicated in chronic inflammation and associated diseases.
  • Protein misfolding mutations and ER stress are linked to inflammatory and autoimmune conditions.
  • The unfolded protein response (UPR) is a hallmark of chronic inflammatory and autoimmune diseases.

Purpose of the Study:

  • To review the intricate relationship between ER stress and inflammation.
  • To elucidate how protein misfolding and UPR activation initiate inflammatory responses.
  • To examine the impact of ER stressors on immune cells and how inflammation affects protein folding.

Main Methods:

  • Literature review synthesizing findings from animal models and human diseases.
  • Analysis of mechanisms by which UPR activation influences inflammation.
  • Examination of environmental ER stressors' effects on antigen-presenting and immune effector cells.

Main Results:

  • Protein misfolding and UPR activation can trigger inflammatory pathways.
  • Environmental ER stressors modulate immune cell function.
  • Inflammatory factors can worsen protein misfolding and ER stress, creating a detrimental cycle.
  • Complex interactions between ER stress and inflammation are evident in various disease models.

Conclusions:

  • ER stress and inflammation are deeply interconnected, influencing disease pathogenesis.
  • Understanding these interactions reveals therapeutic targets for inflammatory and autoimmune diseases.
  • Future research should focus on the bidirectional communication between ER stress and inflammation.