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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

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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

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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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Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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Peroxisomes and Mitochondria01:30

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Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.
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Mitochondria and Endoplasmic Reticulum Imaging by Correlative Light and Volume Electron Microscopy
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The Endoplasmic Reticulum-Mitochondria Encounter Structure Complex Coordinates Coenzyme Q Biosynthesis.

Michal Eisenberg-Bord1, Hui S Tsui2, Diana Antunes3

  • 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.

Contact (Thousand Oaks (Ventura County, Calif.))
|April 3, 2019
PubMed
Summary

Loss of the ERMES complex impairs yeast respiration by destabilizing CoQ synthomes, reducing essential coenzyme Q6 levels. This highlights ER-mitochondria contact sites in regulating mitochondrial function.

Keywords:
ER-mitochondrial encounter structurecoenzyme Qendoplasmic reticulummitochondrion (mitochondria)

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Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) complex is crucial for ER-mitochondria contact sites.
  • Loss of ERMES leads to impaired mitochondrial respiration, but the underlying mechanisms are unclear.

Purpose of the Study:

  • To investigate the molecular basis for impaired respiration in yeast ERMES null mutants.
  • To explore the role of ER-mitochondria contact sites in regulating mitochondrial function and coenzyme Q biosynthesis.

Main Methods:

  • Analysis of mRNA levels for coenzyme Q6 biosynthetic enzymes.
  • Assessment of CoQ synthome stability in ERMES mutants.
  • Fluorescence microscopy to determine spatial relationships between CoQ synthome and ERMES.

Main Results:

  • ERMES null mutants exhibit increased mRNA levels for coenzyme Q6 biosynthetic enzymes.
  • Coenzyme Q6 synthomes are destabilized in ERMES mutants, leading to reduced mitochondrial coenzyme Q6 levels.
  • ERMES and CoQ synthome show close proximity, suggesting spatial coordination.

Conclusions:

  • Destabilization of CoQ synthomes and reduced mitochondrial coenzyme Q6 contribute to impaired respiration in ERMES mutants.
  • ER-mitochondria contact sites, via ERMES, play a role in regulating coenzyme Q6 biogenesis.
  • This study reveals a novel communication pathway between the ER and mitochondria involving coenzyme Q6 biosynthesis.