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Related Concept Videos

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...
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Attachment of Sister Chromatids

As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall of a...
The Mitotic Spindle02:27

The Mitotic Spindle

The mitotic spindle—or spindle apparatus—is a eukaryotic, cytoskeletal structure made up of long protein fibers called microtubules. Formed during cell division, the spindle separates sister chromatids and moves them to opposite ends of a parental cell, where the now individual chromosomes are distributed to two daughter cell nuclei.
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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,...
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: Jun 19, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

Dissecting mitochondria-nucleus contact sites using SPLICS reveals a distributed and dynamic tethering network.

Adamantia Deligiannopoulou1, Lucia Barazzuol1, Caterina Peggion2

  • 1Department of Biomedical Sciences (DSB), University of Padova, Padova, Italy.

Biology Direct
|June 18, 2026
PubMed
Summary
This summary is machine-generated.

Mitochondria-nucleus contact sites are crucial for cell communication but poorly understood. This study reveals a network of proteins, not single tethers, regulates these contacts, highlighting complex inter-organelle communication.

Keywords:
NAMOrganelle communicationProtein kinase A (PKA) and TSPOSPLICSSTOM70

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Analysis of the Mitochondrial Density and Longitudinal Distribution in Rat Live-Skeletal Muscle Fibers by Confocal Microscopy
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Split-Luciferase Reassembly Assay to Measure Endoplasmic Reticulum-Mitochondria Contacts in Live Cells
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Split-Luciferase Reassembly Assay to Measure Endoplasmic Reticulum-Mitochondria Contacts in Live Cells

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Last Updated: Jun 19, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

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Published on: June 16, 2023

Analysis of the Mitochondrial Density and Longitudinal Distribution in Rat Live-Skeletal Muscle Fibers by Confocal Microscopy
10:53

Analysis of the Mitochondrial Density and Longitudinal Distribution in Rat Live-Skeletal Muscle Fibers by Confocal Microscopy

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Split-Luciferase Reassembly Assay to Measure Endoplasmic Reticulum-Mitochondria Contacts in Live Cells
09:09

Split-Luciferase Reassembly Assay to Measure Endoplasmic Reticulum-Mitochondria Contacts in Live Cells

Published on: October 11, 2024

Area of Science:

  • Cell Biology
  • Organelle Biology
  • Inter-organelle Communication

Background:

  • Mitochondria-nucleus contact sites (NAMs) are vital for cellular communication.
  • Their molecular organization and regulation are not well understood.

Purpose of the Study:

  • To quantitatively analyze protein contributions to mitochondria-nucleus contact formation.
  • To identify key tethers and regulatory mechanisms of these contacts.

Main Methods:

  • Utilized split-GFP-based sensors (SPLICSS-P2ANU-MT) in HeLa cells.
  • Employed systematic overexpression and downregulation of candidate proteins.
  • Performed co-expression experiments to investigate cooperative mechanisms.

Main Results:

  • TOM70, MFN2, AKAP95, and PKA catalytic subunit positively modulate contacts upon overexpression.
  • TOM70 downregulation significantly reduces contact sites, suggesting a selective role.
  • TSPO combined with PKA subunits enhances contact formation, indicating synergistic effects.

Conclusions:

  • Mitochondria-nucleus contacts are regulated by a network of interacting proteins, not single dominant tethers.
  • Specific protein partnerships are essential for functional tethering and contact site formation.
  • Understanding these complex regulatory networks is key to deciphering inter-organelle communication.