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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
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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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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The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

15.0K
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,...
15.0K
The Unfolded Protein Response01:37

The Unfolded Protein Response

4.8K
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...
4.8K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

5.8K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
5.8K
Endoplasmic Reticulum01:39

Endoplasmic Reticulum

95.3K
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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Related Experiment Video

Updated: Jul 31, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

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Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside.

Guofang Chen1, Tingyi Wei2,3, Furong Ju4

  • 1Shanghai Key Laboratory of Maternal Fetal Medicine, Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Tongji University School of Medicine, Shanghai, China.

Frontiers in Cell and Developmental Biology
|May 8, 2023
PubMed
Summary
This summary is machine-generated.

The endoplasmic reticulum (ER) protein quality control system maintains cell health. Understanding protein aggregation and ER homeostasis is crucial for diagnosing and treating ER storage diseases.

Keywords:
ERER storage diseasephase transitionprotein aggregateprotein quality control

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4D Imaging of Protein Aggregation in Live Cells
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Assays for the Degradation of Misfolded Proteins in Cells
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Medicine

Background:

  • The endoplasmic reticulum (ER) is vital for protein synthesis, lipid metabolism, and calcium homeostasis.
  • A robust protein quality control (PQC) system in the ER manages misfolded proteins to maintain cellular balance.
  • Failure of ER-PQC leads to protein aggregation, implicated in various human diseases.

Purpose of the Study:

  • To review recent advancements in mammalian ER-PQC.
  • To elucidate the protein phase transition model in ER protein aggregation.
  • To summarize methods for monitoring protein aggregation within the ER.

Main Methods:

  • Literature review of ER protein quality control mechanisms.
  • Discussion of protein phase transition principles.
  • Overview of techniques for observing protein aggregation.

Main Results:

  • Recent advances highlight the complexity of ER-PQC networks.
  • Protein phase transitions offer a model for understanding protein aggregation.
  • Various methods exist to monitor ER protein aggregation.

Conclusions:

  • Comprehensive understanding of ER-PQC and protein aggregation is essential for ER storage disease diagnostics and therapeutics.
  • Enhancing ER-PQC pathways presents a promising therapeutic strategy for ER-related disorders.