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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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Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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

Protein Folding Quality Check in the RER

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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...
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Endoplasmic Reticulum01:39

Endoplasmic Reticulum

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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.
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Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

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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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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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: Oct 2, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

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Deep Learning-Based Morphological Classification of Endoplasmic Reticulum Under Stress.

Yuanhao Guo1,2, Di Shen3, Yanfeng Zhou1,2

  • 1Laboratory of Computational Biology and Machine Intelligence, National Laboratory of Pattern Recognition, Institute of Automation, Chinese Academy of Sciences, Beijing, China.

Frontiers in Cell and Developmental Biology
|February 28, 2022
PubMed
Summary

Endoplasmic reticulum (ER) stress, marked by unfolded protein buildup, can now be identified using a novel image biomarker: ER whorls. A deep learning assay automates the detection of these ER whorls for disease research.

Keywords:
ER stressdeep learninghomeostasisimage biomarkermorphological classification

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Analyzing Mitochondrial Morphology Through Simulation Supervised Learning
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Analyzing Mitochondrial Morphology Through Simulation Supervised Learning
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Analyzing Mitochondrial Morphology Through Simulation Supervised Learning

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Medical Imaging

Background:

  • Endoplasmic reticulum (ER) stress arises from unfolded protein accumulation, disrupting cellular homeostasis.
  • The unfolded protein response (UPR) is activated to restore balance or trigger apoptosis.
  • Chronic ER stress is linked to numerous human diseases, yet reliable image biomarkers are scarce.

Purpose of the Study:

  • To validate a morphological image biomarker for ER stress.
  • To develop a deep learning-based assay for automated detection and analysis of ER stress markers.
  • To provide tools for dissecting disease mechanisms and accelerating drug discovery related to ER stress.

Main Methods:

  • Validated ER whorls (WHs) as a morphological image biomarker for ER stress.
  • Developed ER-WHs-Analyzer, a deep learning assay for automated ER whorl recognition and localization.
  • Utilized a chemical probe for unfolded and aggregated proteins to confirm ER whorl association.

Main Results:

  • ER whorls are specifically associated with the accumulation of unfolded and aggregated proteins.
  • The ER-WHs-Analyzer accurately detects and localizes ER whorls, mimicking expert analysis without manual annotation.
  • The assay reliably classifies ER whorl patterns induced by various ER stress drugs.

Conclusions:

  • ER whorls serve as a validated image biomarker for ER stress.
  • Deep learning effectively identifies complex ER morphological phenotypes, enabling automated analysis.
  • This study offers mechanistic insights and a screening tool for ER stress-related research and drug development.