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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...
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,...
Endoplasmic Reticulum01:39

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer membrane of the nucleus. This structural continuity integrates nuclear and cytoplasmic processes and facilitates efficient intracellular transport. This allows mRNA to move directly from the nucleus to ribosomes for efficient protein synthesis. As a result, the ER serves as a central site for the synthesis, processing, and distribution of...
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...
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...

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Related Experiment Video

Updated: Jun 24, 2026

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP
08:41

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP

Published on: September 6, 2015

[Endoplasmic reticulum stress: light my fIRE].

Marion Bouchecareilh1, Eric Chevet

  • 1Avenir Inserm U889, Université Bordeaux 2, 146, rue Léo Saignat, 33076 Bordeaux, France.

Medecine Sciences : M/S
|April 14, 2009
PubMed
Summary

The Unfolded Protein Response (UPR) protects cells from stress caused by misfolded proteins. This review focuses on IRE1, a key protein in the UPR pathway, exploring its functions and roles in health and disease.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Misfolded proteins in the endoplasmic reticulum (ER) trigger the Unfolded Protein Response (UPR).
  • The UPR is a cellular adaptive mechanism crucial for maintaining proteostasis.
  • Three key proteins mediate the UPR in metazoans: PERK, ATF6, and IRE1.

Purpose of the Study:

  • To review current knowledge on the IRE1 protein, a conserved UPR mediator.
  • To explore the regulatory mechanisms of IRE1.
  • To focus on the physiological and pathophysiological roles of IRE1 signaling pathways.

Main Methods:

  • Literature review of existing research on IRE1.
  • Analysis of crystal structures of IRE1 domains (S. cerevisiae).
  • Synthesis of current understanding of IRE1-dependent signaling.

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

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

Related Experiment Videos

Last Updated: Jun 24, 2026

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP
08:41

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP

Published on: September 6, 2015

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

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

Main Results:

  • IRE1 is the sole UPR-mediating protein conserved across species from yeast to mammals.
  • IRE1 possesses both serine/threonine kinase and endoribonuclease enzymatic activities.
  • Structural insights into IRE1 activation have been gained, but regulatory mechanisms require further exploration.

Conclusions:

  • IRE1 is a critical and highly conserved component of the Unfolded Protein Response.
  • Further research is needed to fully elucidate IRE1's complex regulatory network and its downstream signaling.
  • Understanding IRE1 is vital for comprehending cellular stress responses and its implications in various diseases.