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Related Concept Videos

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

8.9K
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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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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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.3K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
2.3K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

3.3K
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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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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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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Related Experiment Video

Updated: May 10, 2025

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
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Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum

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Clustered Carbon Nanotubes Damage Endoplasmic Reticulum.

Aditya Yadav1, Zhou Fang2, Yuxin Wang1,3

  • 1Department of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati 45267, Ohio, United States.

ACS Applied Materials & Interfaces
|April 20, 2025
PubMed
Summary

Carbon nanotubes (CNTs) can cause nanotoxicity by damaging the endoplasmic reticulum (ER). CNTs aggregate, puncture ER membranes, and increase lipid extraction, leading to ER stress and cellular damage.

Keywords:
carbon nanotubesendoplasmic reticulumlipidsnanotoxicitystructured illumination microscopy

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Facile Preparation of Internally Self-assembled Lipid Particles Stabilized by Carbon Nanotubes
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Repression of Multiple Myeloma Cell Growth In Vivo by Single-wall Carbon Nanotube SWCNT-delivered MALAT1 Antisense Oligos
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Repression of Multiple Myeloma Cell Growth In Vivo by Single-wall Carbon Nanotube SWCNT-delivered MALAT1 Antisense Oligos

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Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
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Facile Preparation of Internally Self-assembled Lipid Particles Stabilized by Carbon Nanotubes
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Area of Science:

  • Nanotechnology
  • Cell Biology
  • Toxicology

Background:

  • Carbon nanotubes (CNTs) offer unique properties and applications.
  • Concerns exist regarding the potential toxicity of CNTs.
  • Understanding CNTs' effects on cellular structures is crucial.

Purpose of the Study:

  • To investigate the nanotoxic effects of CNTs on the endoplasmic reticulum (ER).
  • To elucidate the mechanisms underlying CNT-induced ER damage and stress.

Main Methods:

  • Structure illumination microscopy
  • Transmission electron microscopy
  • RNA sequencing
  • Molecular dynamics simulations
  • Coarse-grained simulations

Main Results:

  • CNTs form clusters during endocytosis, leading to ER fragmentation via puncturing.
  • Up-regulation of activating transcription factor 4 (ATF4), a marker of ER stress, was observed.
  • CNT clustering accelerates lipid extraction, causing significant ER damage.

Conclusions:

  • CNTs induce nanotoxicity by physically damaging the ER structure.
  • CNT-induced ER damage is linked to increased ER stress.
  • Molecular simulations reveal accelerated lipid extraction as a key damage mechanism.