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Related Concept Videos

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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,...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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,...
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...

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Related Experiment Video

Updated: May 23, 2026

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
09:34

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

Published on: December 10, 2016

The ERMES complex and ER-mitochondria connections.

Agnès H Michel1, Benoît Kornmann

  • 1Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland.

Biochemical Society Transactions
|March 23, 2012
PubMed
Summary

Researchers identified a yeast protein complex that mediates contact between the endoplasmic reticulum (ER) and mitochondria. This discovery highlights the crucial role of ER-mitochondria connections in regulating mitochondrial functions.

Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Organelle Communication

Background:

  • Eukaryotic cells require organelle communication for homeostasis.
  • Membrane contact sites facilitate metabolite and information exchange between organelles.
  • The endoplasmic reticulum (ER) and mitochondria are key organelles involved in cellular communication.

Purpose of the Study:

  • To identify naturally occurring protein complexes involved in ER-mitochondria contact sites.
  • To understand the physiological role of ER-mitochondria connections in mitochondrial regulation.
  • To investigate the involvement of Miro GTPases in ER-mitochondria tethering.

Main Methods:

  • Utilized a synthetic protein to artificially tether ER and mitochondria.
  • Isolated and characterized a novel yeast protein complex.

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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain
10:32

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain

Published on: March 4, 2013

Related Experiment Videos

Last Updated: May 23, 2026

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
09:34

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

Published on: December 10, 2016

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain
10:32

Mitochondria-associated ER Membranes (MAMs) and Glycosphingolipid Enriched Microdomains (GEMs): Isolation from Mouse Brain

Published on: March 4, 2013

  • Biochemical analysis to identify components of the protein complex, including Miro GTPases.

    • Main Results:

    • Discovered a yeast protein complex that establishes and maintains ER-mitochondria contact sites.
    • This complex is vital for numerous mitochondrial processes, indicating a regulatory role.
    • Identified Miro GTPases, specifically yeast Gem1, as components of ER-mitochondria connections.
    • Gem1 localizes to the ER-mitochondria interface and affects mitochondrial morphology.

    Conclusions:

    • ER-mitochondria connections are central to regulating mitochondrial biology.
    • Miro GTPases, like Gem1, are key regulators of ER-mitochondria tethering.
    • This finding opens new avenues for understanding organelle communication and mitochondrial function.