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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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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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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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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...
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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...
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Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
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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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Assessing Mitochondrial Function in Sciatic Nerve by High-Resolution Respirometry
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RNA-Binding Proteins Implicated in Mitochondrial Damage and Mitophagy.

Stylianos Ravanidis1, Epaminondas Doxakis1

  • 1Center of Basic Research, Biomedical Research Foundation, Academy of Athens, Athens, Greece.

Frontiers in Cell and Developmental Biology
|June 26, 2020
PubMed
Summary

RNA-binding proteins (RBPs) are crucial for mitochondrial health. Dysfunctional RBPs, like TDP43 and FUS, cause mitochondrial disorders and neurodegenerative diseases.

Keywords:
FUSPUMRNA-binding proteinsTDP43TIA1TIARmitochondriamitophagy

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Molecular Biology

Background:

  • The mitochondrial lifecycle, including biogenesis, fusion, fission, and autophagy, is vital for cellular energy production and function.
  • Mitochondrial dysfunction leads to bioenergetic decline and apoptosis, especially in high-energy-demand cells like neurons and myocytes.
  • RNA-binding proteins (RBPs) regulate mitochondrial gene expression, mRNA processing, stability, and translation, influencing mitochondrial plasticity.

Purpose of the Study:

  • To review the molecular network of disease-relevant RBPs.
  • To highlight the role of RBPs in driving mitochondrial dysfunction in the nervous system.
  • To underscore the link between RBP dysfunction and neurodegenerative pathogenesis.

Main Methods:

  • Review of existing literature on RBPs and mitochondrial function.
  • Focus on specific RBPs: transactive response DNA-binding protein 43 (TDP43), fused in sarcoma (FUS), T-cell intracellular antigen 1 (TIA1), TIA-related protein (TIAR), and pumilio (PUM).
  • Analysis of the connection between RBP misexpression/mutations and mitochondrial impairments.

Main Results:

  • RBPs play a critical role in regulating mitochondrial gene expression and protein synthesis.
  • Dysregulation or mutations in RBPs such as TDP43 and FUS are linked to mitochondrial dysfunction.
  • These mitochondrial impairments are implicated as early events in the pathogenesis of neurological diseases.

Conclusions:

  • RBPs are key players in maintaining mitochondrial homeostasis.
  • Aberrant RBP function is a significant contributor to mitochondrial dysfunction in the nervous system.
  • Targeting RBP-mediated mitochondrial pathways may offer therapeutic strategies for neurodegenerative diseases.