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Related Concept Videos

Endoplasmic Reticulum01:39

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer membrane of the nucleus. This structural continuity integrates nuclear and cytoplasmic processes and facilitates efficient intracellular transport. This allows mRNA to move directly from the nucleus to ribosomes for efficient protein synthesis. As a result, the ER serves as a central site for the synthesis, processing, and distribution of...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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,...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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,...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
ER Retrieval Pathway01:45

ER Retrieval Pathway

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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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 13, 2026

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

Studying endoplasmic reticulum function in vitro using siRNA.

Cornelia M Wilson1, Stephen High

  • 1Faculty of Medicine, University of Limoges, Limoges, France.

Methods in Molecular Biology (Clifton, N.J.)
|April 27, 2010
PubMed
Summary
This summary is machine-generated.

This study investigates the function of oligosaccharyltransferase (OST) subunits in eukaryotic N-glycosylation. Using cell-based assays, researchers identified key roles for ribophorin I and STT3 isoforms in this essential protein modification process.

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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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Last Updated: Jun 13, 2026

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
10:24

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • N-glycosylation is a common protein modification in the endoplasmic reticulum (ER) lumen of eukaryotic cells.
  • The oligosaccharyltransferase (OST) complex facilitates N-glycosylation by transferring oligosaccharides to nascent proteins.
  • The specific functions of individual OST subunits remain largely undefined despite the complex's conserved nature.

Purpose of the Study:

  • To investigate the functional roles of specific OST subunits, including ribophorin I and STT3 isoforms.
  • To elucidate the contribution of these subunits to the N-glycosylation process in vitro.
  • To establish a robust system for studying OST subunit function.

Main Methods:

  • Utilized siRNA-mediated knockdown to reduce the expression of individual OST subunits.
  • Employed a semi-permeabilized mammalian cell system for in vitro analysis.
  • Assessed N-glycosylation of model substrates to evaluate OST activity.

Main Results:

  • Demonstrated the involvement of ribophorin I and STT3 isoforms in OST function.
  • Provided a functional readout for OST subunit activity during N-glycosylation.
  • Validated the utility of the developed cell system for studying OST.

Conclusions:

  • Ribophorin I and STT3 isoforms play crucial roles in the eukaryotic N-glycosylation machinery.
  • The semi-permeabilized cell system offers a versatile platform for dissecting OST complex function.
  • Further research can leverage this system to explore other cellular components and processes.