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Related Concept Videos

The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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The Proteasome02:18

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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The Proteasome02:18

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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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The Proteasome Structure01:17

The Proteasome Structure

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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Related Experiment Video

Updated: Feb 22, 2026

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

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Proteasome impairment by α-synuclein.

Lisa Zondler1, Marcus Kostka2, Patrick Garidel2

  • 1Neurology Department, Ulm University, Ulm, Germany.

Plos One
|September 26, 2017
PubMed
Summary

Alpha-synuclein impairs proteasome function in dopaminergic cells, contributing to Parkinson's disease pathology. This study investigated alpha-synuclein's role in proteasome impairment in various cell types.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Parkinson's disease (PD) is a prevalent neurodegenerative disorder characterized by dopaminergic neuron loss.
  • Alpha-synuclein aggregation in neurons is a hallmark of PD, suggesting its critical role in disease etiology.
  • Proteasome impairment is a potential mechanism of alpha-synuclein toxicity, contributing to protein aggregate formation.

Purpose of the Study:

  • To investigate the direct impact of alpha-synuclein on proteasome function.
  • To determine if alpha-synuclein impairs proteasome activity in a cell-type-specific manner.

Main Methods:

  • In vitro assays using recombinant alpha-synuclein and isolated proteasomes.
  • In vivo studies involving transient and stable expression of alpha-synuclein in different cell lines (U2OS, SH-SY5Y, PC12).
  • Assessment of proteasome activity, specifically the chymotrypsin-like cleavage function.

Main Results:

  • Recombinant alpha-synuclein oligomers and fibrils showed minimal impairment of isolated 20S proteasome function in vitro.
  • Transient alpha-synuclein expression in U2OS cells did not significantly affect proteasome activity.
  • Stable expression of alpha-synuclein in dopaminergic SH-SY5Y and PC12 cells led to significant impairment of 20S/26S proteasome activity.

Conclusions:

  • Alpha-synuclein's impairment of proteasome function is dependent on the cellular context.
  • Dopaminergic cells exhibit selective vulnerability to alpha-synuclein pathology due to impaired proteasome processing.
  • This suggests a mechanism contributing to the selective loss of dopaminergic neurons in Parkinson's disease.