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Related Concept Videos

Endoplasmic Reticulum01:39

Endoplasmic Reticulum

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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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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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Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

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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.
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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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Protein Networks02:26

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Related Experiment Video

Updated: Feb 14, 2026

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
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Endoplasmic Reticulum Network Formation with Xenopus Egg Extracts.

Songyu Wang1, Fabian B Romano1, Tom A Rapoport2

  • 1Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115 songyuwang.sw@gmail.com Fabian_Romano-Chernac@hms.harvard.edu.

Cold Spring Harbor Protocols
|February 25, 2018
PubMed
Summary

Researchers developed protocols to assemble endoplasmic reticulum (ER) networks in Xenopus egg extracts. These extracts, arrested at different cell cycle stages, allow in vitro ER network formation similar to tissue culture cells.

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Area of Science:

  • Cell Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER) forms a complex tubular network with three-way junctions, essential in all eukaryotic cells.
  • Xenopus laevis egg extracts contain components for in vitro ER network assembly.

Purpose of the Study:

  • To provide protocols for assembling ER networks in Xenopus egg extracts arrested at specific cell cycle stages (interphase or metaphase).
  • To enable biochemical manipulation and study of ER network formation.

Main Methods:

  • Utilizing Xenopus laevis egg extracts arrested in interphase (via calcium release and cycloheximide) or metaphase (using a calcium chelator).
  • Developing specific procedures for ER network assembly within these arrested extracts.

Main Results:

  • Successfully assembled ER networks in vitro that closely resemble those found in tissue culture cells.
  • Demonstrated the utility of the extracts for biochemical manipulation, including testing effects of proteins, small molecules, or component depletion.

Conclusions:

  • Xenopus egg extracts provide a versatile system for studying ER network assembly and function.
  • The developed protocols facilitate biochemical investigations into the mechanisms of ER network formation.