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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...
Golgi Apparatus01:49

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

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...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...

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Related Experiment Video

Updated: Jun 29, 2026

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain
10:32

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain

Published on: March 4, 2013

Coatomer-rich endoplasmic reticulum

L Orci1, A Perrelet, M Ravazzola

  • 1Department of Morphology, University of Geneva Medical School, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|December 6, 1994
PubMed
Summary
This summary is machine-generated.

Researchers discovered two distinct transitional endoplasmic reticulum (ER) sites in normal cells: the Sec23p complex and the coatomer-rich ER. The coatomer-rich ER overexpressed when ER-to-Golgi transport was reduced.

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Mitochondria and Endoplasmic Reticulum Imaging by Correlative Light and Volume Electron Microscopy
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Mitochondria and Endoplasmic Reticulum Imaging by Correlative Light and Volume Electron Microscopy

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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

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Related Experiment Videos

Last Updated: Jun 29, 2026

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain
10:32

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain

Published on: March 4, 2013

Mitochondria and Endoplasmic Reticulum Imaging by Correlative Light and Volume Electron Microscopy
09:21

Mitochondria and Endoplasmic Reticulum Imaging by Correlative Light and Volume Electron Microscopy

Published on: July 20, 2019

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • The endoplasmic reticulum (ER) is a key organelle for protein synthesis and modification.
  • ER-to-Golgi transport is crucial for cellular function and protein homeostasis.

Purpose of the Study:

  • To identify and characterize distinct functional sites within the transitional endoplasmic reticulum.
  • To investigate the relationship between ER-to-Golgi transport and the composition of transitional ER elements.

Main Methods:

  • Cellular fractionation and protein complex localization studies.
  • Experimental manipulation of ER-to-Golgi transport rates.

Main Results:

  • Identification of two distinct transitional ER sites: the classical transitional element (Sec23p complex) and a novel coatomer-rich ER.
  • Demonstration that the coatomer-rich ER is overexpressed under conditions of reduced ER-to-Golgi transport.

Conclusions:

  • Normal cells possess at least two distinct types of transitional ER sites with different protein compositions.
  • The coatomer-rich ER is dynamically regulated and responds to changes in anterograde protein transport from the ER.