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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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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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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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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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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...
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Golgi Apparatus01:49

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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.
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Updated: Mar 19, 2026

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
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Shaping the Endoplasmic Reticulum into a Social Network.

Hong Zhang1, Junjie Hu1

  • 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Trends in Cell Biology
|June 25, 2016
PubMed
Summary

Integral membrane proteins shape the endoplasmic reticulum (ER) network in eukaryotic cells. This review explores protein modules, mechanisms, and cellular functions related to ER morphology and its role in multicellular development.

Keywords:
endoplasmic reticulummembrane fusionmembrane shapingmulticellular developmentorganelle contacts

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • The endoplasmic reticulum (ER) forms a complex network of tubules and sheets within eukaryotic cells, maintaining a continuous membrane system.
  • Integral membrane proteins are known to play a crucial role in shaping the ER's distinctive morphology.

Purpose of the Study:

  • To review common protein modules and mechanisms responsible for generating the characteristic shape of the ER.
  • To discuss cellular functions linked to ER morphology, including inter-organelle contacts.
  • To explore the potential roles of ER morphology in the development of multicellular organisms.

Main Methods:

  • Literature review of studies on ER morphology and membrane dynamics.
  • Analysis of functional studies involving mutant proteins affecting ER shape.
  • Discussion of protein modules and cellular mechanisms involved in ER shaping.

Main Results:

  • Identified common protein modules and mechanisms that dictate ER structure.
  • Highlighted the significance of ER morphology and membrane dynamics through functional studies.
  • Emphasized the importance of ER contacts with other membrane systems.

Conclusions:

  • Protein modules and specific mechanisms are key to establishing and maintaining ER architecture.
  • ER morphology is intrinsically linked to vital cellular functions and organismal development.
  • Understanding ER shape provides insights into cellular processes and multicellular organism development.