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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...
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...
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...
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.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Replicative Cell Senescence02:15

Replicative Cell Senescence

Replicative cell senescence is a property of cells that allows them to divide a finite number of times throughout the organism's lifespan while preventing excessive proliferation. Replicative senescence is associated with the gradual loss of the telomere — short, repetitive DNA sequences found at the end of the chromosomes. Telomeres are bound by a group of proteins to form a protective cap on the ends of chromosomes. Embryonic stem cells express telomerase — an enzyme that adds the telomeric...

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Updated: May 9, 2026

Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

IRE1: ER stress sensor and cell fate executor.

Yani Chen1, Federica Brandizzi

  • 1MSU-DOE Plant Research Laboratory and Department of Plant Biology, Michigan State University, 612 Wilson Rd, Room 122, East Lansing, MI 48824, USA.

Trends in Cell Biology
|July 25, 2013
PubMed
Summary

The unfolded protein response (UPR) uses Inositol-requiring enzyme 1 (IRE1) to maintain endoplasmic reticulum (ER) function. This review updates the IRE1 signaling model, comparing its roles across species and exploring future research directions.

Keywords:
ER stressIRE1cell fatemembrane trafficking systemprotein quality controlunfolded protein response

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Area of Science:

  • Cellular biology
  • Molecular biology
  • Biochemistry

Background:

  • Cells utilize the unfolded protein response (UPR) to manage endoplasmic reticulum (ER) protein-folding stress.
  • Inositol-requiring enzyme 1 (IRE1) is a key ER transmembrane sensor that orchestrates the UPR.
  • While promoting cell survival, mammalian IRE1 can also trigger apoptosis by degrading anti-apoptotic microRNAs.

Purpose of the Study:

  • To present an updated model of IRE1 signaling.
  • To explore novel mechanisms of IRE1 sensing.
  • To compare IRE1 characteristics across different species.

Main Methods:

  • Literature review and synthesis.
  • Comparative analysis of IRE1 function in various organisms.
  • Discussion of emerging research trends.

Main Results:

  • IRE1 plays a conserved yet distinct role in cellular homeostasis across species.
  • Emerging sensing mechanisms for IRE1 are being uncovered.
  • The dual role of IRE1 in promoting survival and apoptosis is highlighted.

Conclusions:

  • IRE1 is a critical regulator of ER function and cellular fate.
  • Understanding IRE1 signaling is crucial for cellular homeostasis.
  • Further research into IRE1 mechanisms promises new insights into UPR and disease.