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Related Concept Videos

Maturation of Endosomes01:28

Maturation of Endosomes

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The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
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The Endoplasmic Reticulum01:43

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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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The Early Endosome: Endocytosis of Transferrin01:28

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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Introduction to Membrane Traffic01:44

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The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
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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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Golgi Apparatus01:09

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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.
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Related Experiment Video

Updated: Nov 18, 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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Mobile late endosomes modulate peripheral endoplasmic reticulum network architecture.

Menno Spits1, Iris T Heesterbeek1, Lennard M Voortman1

  • 1Division of Cell and Chemical Biology, Oncode Institute, Leiden University Medical Centre, Leiden, The Netherlands.

EMBO Reports
|February 8, 2021
PubMed
Summary
This summary is machine-generated.

Late endosomes and lysosomes control the endoplasmic reticulum (ER) network architecture through a process called ER hitchhiking. Restricted movement of these organelles limits ER dynamics and peripheral network complexity.

Keywords:
endoplasmic reticulumlate endosomesmembrane contact sitesorganelle hitchhikingstarvation

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Area of Science:

  • Cell Biology
  • Organelle Dynamics

Background:

  • The endoplasmic reticulum (ER) is a vast organelle crucial for cellular processes, interacting with numerous other organelles.
  • Understanding how the ER network architecture is maintained and remodeled, particularly in the cell periphery, is essential for cell function.

Purpose of the Study:

  • To investigate the influence of other organelles on the ER network architecture in the cell periphery.
  • To elucidate the role of late endosomes and lysosomes in shaping the ER network.

Main Methods:

  • Live-cell imaging techniques to observe ER dynamics and organelle co-migration.
  • Genetic and chemical perturbations to disrupt late endosomal movement and tethering proteins.

Main Results:

  • Identified 'ER hitchhiking,' the co-migration of ER with late endosomes and lysosomes, as a key mechanism controlling ER network architecture.
  • Demonstrated that fusion of emerging ER structures with existing tubules alters local ER architecture.
  • Showed that restricted late endosomal movement, such as during cell starvation or depletion of tether proteins, reduces ER dynamics and peripheral network complexity.

Conclusions:

  • Late endosomal and lysosomal positioning and mobility are directly coupled to ER network architecture.
  • ER network architecture is dynamically controlled by the movement of late endosomes and lysosomes, highlighting a novel inter-organelle communication pathway.