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Related Concept Videos

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,...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
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,...

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Related Experiment Video

Updated: Jun 12, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

Mitochondria directly interact with the nuclear pore complex.

Ivan Menendez-Montes1,2, Consuelo Marin-Vicente3,4, Shibani Mukherjee2,5

  • 1Department of Medicine/Cardiology, University of Arizona, Tucson, AZ, USA.

Nature
|June 10, 2026
PubMed
Summary
This summary is machine-generated.

Mitochondria directly interact with nuclear pores via VDAC1 and RANBP2, impacting nuclear energy levels and cellular differentiation. This novel mitochondria-nucleus proximity is crucial for cell function and development.

More Related Videos

Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue
09:27

Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue

Published on: March 23, 2015

Related Experiment Videos

Last Updated: Jun 12, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue
09:27

Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue

Published on: March 23, 2015

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitochondria and organelles interact, notably with the endoplasmic reticulum at mitochondrial-associated membranes.
  • Previous research indicated mitochondria-nuclear membrane contacts in specific cell types.

Purpose of the Study:

  • To investigate direct interactions between mitochondria and nuclear pores.
  • To elucidate the functional consequences of mitochondria-nuclear pore complex interactions.

Main Methods:

  • Utilized unbiased proteomic screens (GST pulldown, BioID) to identify interacting proteins.
  • Performed in vitro experiments including CRISPR knockout, protein truncation, and site-directed mutagenesis.
  • Conducted in vivo studies in mice.

Main Results:

  • Identified VDAC1 (voltage-dependent anion channel 1) on mitochondria interacting with RANBP2 (Ran-binding protein 2) on nuclear pores.
  • Disruption of VDAC1-RANBP2 interaction reduced mitochondria-nucleus proximity, nuclear ATP, and phosphocreatine levels.
  • Observed decreased nuclear phosphoproteome and downregulated pathways in histone modification, differentiation, and transcription.
  • In vivo deletion of RANBP2 C-terminal domain led to embryonic lethality with cardiac and neural crest defects.

Conclusions:

  • Established a novel mechanism of direct mitochondria-nuclear pore complex interaction.
  • This interaction is critical for regulating nuclear energetics and cellular differentiation.
  • The findings highlight a new layer of organelle crosstalk essential for development.