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Related Concept Videos

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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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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Protein Translocation Machinery on the ER Membrane01:28

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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Export of Misfolded Proteins out of the ER01:32

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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...
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Related Experiment Video

Updated: Jun 7, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Visualizing ER-phagy and ER architecture in vivo.

Yongjuan Sang1,2, Boran Li1, Tinglin Su1

  • 1International Institutes of Medicine, The Fourth Affiliated Hospital of Zhejiang University School of Medicine , Yiwu, China.

The Journal of Cell Biology
|November 18, 2024
PubMed
Summary
This summary is machine-generated.

Researchers developed new mouse models to study ER-phagy (endoplasmic reticulum autophagy). These models reveal how ER-phagy varies across the body and changes during stress, offering insights into cellular health.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • ER-phagy is vital for cellular homeostasis but its variations and disease relevance are unclear.
  • Quantifiable in vivo methods are needed to study ER structure and ER-phagy dynamics.
  • Existing knowledge gaps hinder understanding of ER-phagy's role in different cell types and pathologies.

Purpose of the Study:

  • To develop novel reporter mouse models for visualizing and quantifying ER-phagy and ER architecture in vivo.
  • To investigate the spatiotemporal variations of ER-phagy across different organs and tissues.
  • To explore the remodeling of ER-phagy and ER network under various stress conditions.

Main Methods:

  • Generation of two transgenic mouse lines expressing an ER lumen-targeting tandem RFP-GFP (ER-TRG) tag.
  • Constitutive and conditional expression of the ER-TRG tag for precise temporal control.
  • Systemic analysis of ER-phagy and ER structure in vivo and ex vivo across diverse organs, tissues, and primary cultures.

Main Results:

  • Significant variations in basal ER-phagy levels were observed across different organs and tissues.
  • ER-phagy and ER network architecture undergo substantial remodeling under stress conditions like starvation and injury.
  • The ER-TRG reporter system allows for single-cell resolution measurements of ER-phagy in vivo.

Conclusions:

  • The developed ER-TRG reporter mouse models are valuable tools for studying ER-phagy.
  • These models facilitate fundamental research into cellular homeostasis and ER dynamics.
  • The findings have broad applications in translational studies for various diseases.