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Related Concept Videos

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.
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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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.
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Porin Insertion in the Outer Mitochondrial Membrane01:12

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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.
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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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Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
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Brain clusterin protein isoforms and mitochondrial localization.

Sarah K Herring1, Hee-Jung Moon1, Punam Rawal1

  • 1Department of Pharmacology and Toxicology, School of Pharmacy, University of Kansas, Lawrence, United States.

Elife
|November 19, 2019
PubMed
Summary

Clusterin (CLU) has a newly discovered mitochondrial isoform, mitoCLU, found in neurons and astrocytes. This finding is crucial for understanding Alzheimer's disease (AD) and CLU's role in its development.

Keywords:
apolipoprotein J (ApoJ)clusterin (CLU)humanlate-onset Alzheimer's disease (LOAD)mitochondriamouseneuroscience

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Area of Science:

  • Neuroscience
  • Genetics
  • Molecular Biology

Background:

  • Clusterin (CLU), also known as apolipoprotein J (ApoJ), is a significant genetic risk factor for late-onset Alzheimer's disease (LOAD).
  • The precise mechanisms by which CLU influences LOAD pathogenesis remain incompletely understood.
  • Investigating CLU's diverse forms and functions is critical for advancing LOAD research.

Purpose of the Study:

  • To identify and characterize novel isoforms of Clusterin (CLU) in the brain.
  • To determine the subcellular localization and expression patterns of these CLU isoforms in neural cells.
  • To elucidate the potential role of a specific CLU isoform in the context of Alzheimer's disease.

Main Methods:

  • Utilized multiple rodent and human brain tissue and neural cell models.
  • Employed techniques to identify and localize different CLU protein isoforms.
  • Analyzed gene and protein expression levels, including in CLU knockout models.

Main Results:

  • Demonstrated that CLU is expressed as multiple isoforms with distinct cellular and subcellular localizations in the brain.
  • Identified a novel non-glycosylated 45 kDa CLU isoform, termed mitoCLU, localized to the mitochondrial matrix in both rodent and human neurons and astrocytes.
  • Revealed that rodent mitoCLU is translated from a non-canonical CUG start site in Exon 3, distinct from the human AUG start site, and confirmed its presence in CLU knockout models.

Conclusions:

  • The discovery of mitoCLU provides foundational knowledge for understanding CLU's multifaceted role in the brain.
  • This isoform's unique localization and translation mechanism offer new avenues for investigating its involvement in LOAD.
  • Further research into mitoCLU function is essential for elucidating the relationship between CLU and Alzheimer's disease development.