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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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The Endoplasmic Reticulum01:43

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Endoplasmic Reticulum01:39

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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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The Unfolded Protein Response01:37

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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...
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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...
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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UFMylation: A Key Role in Maintaining Endoplasmic Reticulum Homeostasis.

Kang Zheng1, Yi Ai1, Junlin Yang1

  • 1College of Life and Environmental Sciences, Hangzhou Normal University, Zhejiang, Hangzhou, China.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|March 19, 2026
PubMed
Summary
This summary is machine-generated.

UFMylation, a key ER process, regulates cell stress by clearing damaged components. Its dysregulation links to diseases involving ER dysfunction.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • UFMylation is a ubiquitin-like post-translational modification crucial for endoplasmic reticulum (ER) function.
  • Core components include UFM1, UBA5, UFC1, UFL1, DDRGK1, and CDK5RAP3.
  • The UFL1-DDRGK1 complex at the ER manages substrate modification.

Purpose of the Study:

  • To review the molecular pathways of ER-associated UFMylation.
  • To discuss UFMylation's regulatory roles in ER function and stress response.
  • To explore UFMylation's involvement in congenital human diseases.

Main Methods:

  • Literature review of UFMylation pathways.
  • Analysis of UFMylation's role in ER proteostasis and quality control.
  • Examination of disease associations with UFMylation dysregulation.

Main Results:

  • UFMylation modulates ER stress, balancing cell remodeling and apoptosis.
  • It coordinates ER-phagy and ribosome-associated quality control for ER integrity.
  • UFMylation targets key proteins to remove stalled ribosomes and damaged ER.

Conclusions:

  • UFMylation is essential for maintaining ER proteostasis and structural integrity.
  • Dysregulation of UFMylation is linked to diseases with impaired ER function.
  • Understanding UFMylation pathways may offer insights into congenital diseases.