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Related Concept Videos

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

16.8K
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,...
16.8K
Endoplasmic Reticulum01:39

Endoplasmic Reticulum

102.0K
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.
102.0K
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

6.7K
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...
6.7K
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

6.1K
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
6.1K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

6.3K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
6.3K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

4.2K
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...
4.2K

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Related Experiment Video

Updated: Oct 18, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

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Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases.

Hannah T Perkins1,2, Viki Allan1

  • 1Division of Molecular and Cellular Function, School of Biological Sciences, Michael Smith Building, The University of Manchester, Dover Street, Manchester M13 9PT, UK.

Cells
|September 28, 2021
PubMed
Summary
This summary is machine-generated.

The endoplasmic reticulum (ER) has complex structures and movements crucial for cell function. Disruptions in ER morphology and dynamics are linked to diseases and pathogen infections.

Keywords:
anomalous diffusiondynamicsdyneinendoplasmic reticulum (ER)kinesinmembrane contact site (MCS)microtubulemorphology

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

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Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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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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Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum

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Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
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Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER) is a vital organelle with a complex network of tubules and sheets connected to the nuclear envelope.
  • ER morphology and dynamics are increasingly recognized as critical determinants of its diverse cellular functions.
  • Alterations in ER structure and movement are implicated in various diseases and pathogen interactions.

Purpose of the Study:

  • To review current understanding of endoplasmic reticulum morphology, including functional subdomains and membrane contact sites.
  • To discuss the dynamics of the ER, focusing on methods for quantifying its movement.
  • To explore the links between ER morphology, dynamics, and associated diseases and pathogen exploitation.

Main Methods:

  • Literature review of studies on ER structure, dynamics, and function.
  • Analysis of research linking ER protein mutations to disease pathogenesis.
  • Examination of mechanisms by which pathogens manipulate ER.

Main Results:

  • ER morphology comprises interconnected tubules and sheet-like regions, forming specialized functional subdomains and membrane contact sites.
  • ER dynamics involve complex movements crucial for cellular processes, with ongoing efforts to quantify this motion.
  • Dysregulation of ER morphology and dynamics is associated with neurodegenerative diseases (Alzheimer's, Parkinson's, ALS) and pathogen replication.

Conclusions:

  • The intricate morphology and dynamic nature of the endoplasmic reticulum are fundamental to its cellular roles.
  • Understanding ER structure-function relationships is key to deciphering disease mechanisms and developing therapeutic strategies.
  • Targeting ER pathways presents potential avenues for combating diseases and infectious agents.