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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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Assembly of the Lipid Bilayer in the ER01:28

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Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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Tail-anchoring of Proteins in the ER Membrane01:45

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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

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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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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 in vitro.

Csilla-Maria Ferencz1, Gernot Guigas1, Andreas Veres1

  • 1Experimental Physics I, University of Bayreuth, D-95440 Bayreuth, Germany.

Biochimica Et Biophysica Acta
|June 12, 2016
PubMed
Summary
This summary is machine-generated.

The endoplasmic reticulum (ER) forms complex networks. Reconstituting ER networks in vitro reveals that substrate interactions significantly alter their structure, unlike in vivo networks.

Keywords:
ER networkER reconstitutionEndoplasmic reticulumIn vitro assayMicrosomesSelf-assemblyThree-way junctions

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Area of Science:

  • Cell Biology
  • Biophysics
  • Biochemistry

Background:

  • Eukaryotic organelles, like the endoplasmic reticulum (ER), exhibit complex, non-spherical shapes.
  • The ER forms an extensive network of membrane tubules crucial for cellular functions.
  • Understanding ER network morphogenesis is incomplete, particularly the role of the surrounding environment.

Purpose of the Study:

  • To investigate the influence of the host substrate on endoplasmic reticulum (ER) network formation in vitro.
  • To compare in vitro reconstituted ER networks with native ER networks in vivo.
  • To elucidate the self-assembly mechanisms governing ER network geometry.

Main Methods:

  • Observation of ER networks in cultured mammalian cells (in vivo).
  • Reconstitution of ER networks from purified ER microsomes on various substrates (glass, gels).
  • Self-assembly experiments using ER microsomes on oil droplets.

Main Results:

  • In vivo ER networks show narrow tubule length distributions (mean ~1μm) and predominantly three-way junctions.
  • In vitro networks on flat substrates exhibit broader length distributions and longer mean tubule lengths.
  • ER networks reconstituted on oil droplets closely mimic the geometry of native cellular ER networks.

Conclusions:

  • The inherent self-assembly capacity of ER microsomes can generate native-like network geometry when substrate influence is minimized.
  • Substrate interactions significantly impact ER network structure and geometry in vitro.
  • The preference for three-way junctions may arise from the fusion of protein-induced curved vesicles, forming 'starfish-shaped' structures.