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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...
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,...
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,...
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...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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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Updated: May 26, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

MICOS and MIMAS, multifunctional assemblies linking mitochondrial biogenesis, architecture, and function.

Patrick Horten1,2, Kuo Song1, Nikolaus Pfanner1,3

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

Protein Science : a Publication of the Protein Society
|May 25, 2026
PubMed
Summary
This summary is machine-generated.

Mitochondrial cristae organization is key for energy production. This review highlights the MICOS and MIMAS protein complexes, crucial for inner mitochondrial membrane structure and function.

Keywords:
cristaemembrane organizationmetabolismmitochondriarespiratory chain

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Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
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Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

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Related Experiment Videos

Last Updated: May 26, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
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Published on: June 16, 2023

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
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A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

Area of Science:

  • Mitochondrial biology
  • Cellular physiology
  • Biochemistry

Background:

  • Mitochondrial cristae architecture is essential for efficient oxidative phosphorylation and overall mitochondrial health.
  • The inner mitochondrial membrane's complex structure is maintained by protein complexes that create distinct subcompartments, ensuring functional asymmetry.
  • Recent research has significantly advanced our understanding of the mechanisms governing inner mitochondrial membrane organization and dynamics.

Purpose of the Study:

  • To review the roles of the mitochondrial contact site and cristae organizing system (MICOS) in stabilizing cristae entry gates.
  • To discuss the newly identified mitochondrial multifunctional assembly (MIMAS) and its contribution to inner membrane organization.
  • To provide insights into how these protein complexes collectively organize the inner mitochondrial membrane.

Main Methods:

  • Literature review of recent studies on mitochondrial inner membrane organization.
  • Analysis of the structural and functional roles of MICOS and MIMAS.
  • Synthesis of current knowledge on protein complexes involved in membrane compartmentalization and dynamics.

Main Results:

  • MICOS complex is identified as a key player in maintaining the structural integrity of cristae junctions.
  • MIMAS emerges as a novel megacomplex involved in organizing the inner mitochondrial membrane.
  • Both MICOS and MIMAS contribute to the functional compartmentalization and dynamics of the inner membrane.

Conclusions:

  • MICOS and MIMAS are critical protein assemblies for organizing mitochondrial cristae and the inner membrane.
  • Understanding these complexes is vital for comprehending mitochondrial physiology and potential therapeutic targets.
  • Further research into MICOS, MIMAS, and their interactions will illuminate mitochondrial function in health and disease.