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Related Concept Videos

Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

2.4K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
5.0K
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

4.7K
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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Mitochondrial Membranes01:45

Mitochondrial Membranes

17.2K
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,...
17.2K
Membrane Transporters01:31

Membrane Transporters

18.2K
Transporters are essential membrane transport proteins with functions related to cell nutrition, homeostasis, communication, etc. Approximately 7% of all genes in the human genome code for transporters or transporter-related proteins.
Transporters are mainly composed of alpha-helices, built from bundles of ten or more helices traversing the plasma membrane. The solute-binding sites are located midway, where some of the helices are broken or distorted, making space for the binding site through...
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Related Experiment Video

Updated: Feb 11, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes.

Thomas Becker1,2, Richard Wagner3

  • 1Faculty of Medicine, Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, D-79104, Germany.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|May 1, 2018
PubMed
Summary

Mitochondrial outer membrane transport is more complex than previously thought, with multiple channels regulating the passage of proteins and molecules. This challenges the idea of the outer membrane being a simple filter.

Keywords:
MIM complexSAM complexTOM complexVDACmitochondria

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Neuromodulation and Mitochondrial Transport: Live Imaging in Hippocampal Neurons over Long Durations
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Immunodetection of Outer Membrane Proteins by Flow Cytometry of Isolated Mitochondria
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Immunodetection of Outer Membrane Proteins by Flow Cytometry of Isolated Mitochondria

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Related Experiment Videos

Last Updated: Feb 11, 2026

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Neuromodulation and Mitochondrial Transport: Live Imaging in Hippocampal Neurons over Long Durations
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Immunodetection of Outer Membrane Proteins by Flow Cytometry of Isolated Mitochondria
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Immunodetection of Outer Membrane Proteins by Flow Cytometry of Isolated Mitochondria

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Area of Science:

  • Mitochondrial biology
  • Membrane transport
  • Cellular physiology

Background:

  • Mitochondrial function relies on transport across inner and outer membranes.
  • Outer membrane transport mechanisms are less understood than inner membrane processes.
  • Traditionally, the outer membrane was viewed as a non-specific filter.

Purpose of the Study:

  • To review the diverse functions, selectivity, and regulation of mitochondrial outer membrane channels.
  • To highlight recent findings on protein-conducting channels and other transporters.
  • To challenge the established view of the outer membrane's permeability.

Main Methods:

  • Literature review of recent studies on mitochondrial outer membrane channels.
  • Analysis of known and putative channel functions.
  • Synthesis of current understanding of mitochondrial transport.

Main Results:

  • Four distinct protein-conducting channels exist in the outer mitochondrial membrane.
  • The voltage-dependent anion channel (VDAC) is the primary channel for small hydrophilic molecules.
  • Three additional channels with unknown substrate specificity have been identified.

Conclusions:

  • The mitochondrial outer membrane possesses diverse and specific transport mechanisms.
  • Multiple channel proteins contribute to outer membrane permeability.
  • The outer membrane is not merely an unspecific size-exclusion filter.