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Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

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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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The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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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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Structure of Porins01:21

Structure of Porins

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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...
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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...
4.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

10.1K
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,...
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

4.4K
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...
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Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
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Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

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Mitochondrial outer membrane permeabilization at the single molecule level.

Shashank Dadsena1, Andreas Jenner1,2, Ana J García-Sáez3

  • 1Institute for Genetics, CECAD Research Center, University of Cologne, Cologne, Germany.

Cellular and Molecular Life Sciences : CMLS
|February 12, 2021
PubMed
Summary
This summary is machine-generated.

Mitochondrial outer membrane permeabilization (MOMP) regulates programmed cell death, crucial for health and disease. Single-molecule studies reveal the intricate protein interactions controlling this vital process.

Keywords:
ApoptosisBcl-2 proteinsMitochondrial outer membrane permeabilization (MOMP)Single-molecule techniques

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Apoptotic cell death is fundamental for development, immunity, and tissue balance.
  • Dysregulation of apoptosis is implicated in numerous diseases.
  • Mitochondrial outer membrane permeabilization (MOMP) is a key step in the intrinsic apoptotic pathway.

Purpose of the Study:

  • To review current understanding of MOMP regulation.
  • To highlight the role of Bcl-2 family proteins and other regulatory factors.
  • To emphasize the utility of single-molecule techniques in studying MOMP.

Main Methods:

  • Review of existing literature on MOMP regulation.
  • Focus on the protein interaction network of the Bcl-2 family.
  • Analysis of studies employing single-molecule techniques to investigate MOMP-related protein complexes.

Main Results:

  • MOMP regulation involves a complex network of Bcl-2 family proteins and other elements.
  • Single-molecule techniques are crucial for resolving spatial and temporal complexities of MOMP.
  • Key single-molecule studies have elucidated the composition, assembly, and structure of regulatory protein complexes.

Conclusions:

  • Understanding MOMP regulation is critical for comprehending cell death pathways and associated diseases.
  • The Bcl-2 family network plays a central role in controlling MOMP.
  • Advanced single-molecule approaches provide unprecedented insights into the molecular mechanisms governing MOMP.