Related Experiment Video
Updated: Jun 23, 2025
07:35
Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
Published on: June 1, 2022
2.2K
Permeabilization of the outer mitochondrial membrane: Mechanisms and consequences
Maria A Yapryntseva1, Boris Zhivotovsky2, Vladimir Gogvadze3
1Engelhardt Institute of Molecular Biology, RAS, 119991 Moscow, Russia; Faculty of Medicine, Lomonosov Moscow State University, 119192 Moscow, Russia.
Summary
Mitochondrial outer membrane permeabilization is a key process in cell death, regulating molecule passage and cell fate. This review details pore types, activation mechanisms, and disease relevance.
Area of Science:
- Cell Biology
- Biochemistry
- Pathology
Background:
- The outer mitochondrial membrane (OMM) regulates cellular processes, including energy production and cell death.
- OMM permeabilization allows passage of small molecules and is critical for various cell death pathways.
- Dysregulation of OMM permeabilization is implicated in numerous diseases.
Purpose of the Study:
- To provide a comprehensive review of outer mitochondrial membrane permeabilization.
- To discuss the distinct types of pores, their activation mechanisms, and physiological/pathological roles.
- To explore the involvement of OMM permeabilization in various disease states.
Main Methods:
- Literature review of scientific articles on mitochondrial outer membrane permeabilization.
- Analysis of mechanisms underlying pore formation and activation.
- Synthesis of information on the role of OMM permeabilization in different diseases.
Main Results:
- Identified distinct pore types in the OMM, each activated by specific stimuli.
- Elucidated diverse mechanisms controlling OMM permeabilization.
- Highlighted the critical role of OMM permeabilization in autophagy, apoptosis, and necroptosis.
- Demonstrated the involvement of OMM permeabilization in the pathogenesis of various diseases.
Conclusions:
- OMM permeabilization is a tightly regulated process with significant physiological and pathological implications.
- Understanding OMM permeabilization mechanisms offers therapeutic targets for diseases involving cell death pathways.
- Further research into OMM permeabilization is crucial for advancing disease treatment strategies.
More Related Videos
Related Concept Videos
01:45Mitochondrial Membranes
9.9K
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,...
9.9K
01:21Structure of Porins
3.0K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K
01:12Porin Insertion in the Outer Mitochondrial Membrane
3.0K
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...
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...
3.0K
01:28The Inner Mitochondrial Membrane
3.3K
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...
3.3K
01:19Translocation of Proteins into the Mitochondria
3.1K
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,...
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,...
3.1K
01:34Protein Transport into the Inner Mitochondrial Membrane
3.7K
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...
Transport of mitochondrial precursors across the TIM23 channel is driven by...
3.7K