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Related Concept Videos

Huntington Disease l: Introduction01:21

Huntington Disease l: Introduction

Huntington disease or HD is a progressive, fatal neurodegenerative disorder inherited in an autosomal dominant pattern.PathophysiologyIt is caused by expansion of the CAG trinucleotide repeat in the HTT gene on chromosome 4 (4p16.3), producing an abnormal huntingtin protein with an expanded polyglutamine tract. This misfolded protein disrupts cellular function, leading to neuronal death. Normal alleles have ≤26 repeats, 27–35 are intermediate (risk of expansion), 36–39 show reduced penetrance,...
The Proteasome01:13

The Proteasome

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 (ubiquitin...
The Proteasome02:18

The Proteasome

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.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome02:18

The Proteasome

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.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

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Related Experiment Video

Updated: Jun 6, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
07:08

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

Proteasomal dysfunction in aging and Huntington disease.

Xiao-Jiang Li1, Shihua Li

  • 1Department of Human Genetics, Emory University School of Medicine, Atlanta, GA 30322, USA. xli2@emory.edu

Neurobiology of Disease
|December 15, 2010
PubMed
Summary

Protein degradation is vital for cell health. This review explores how aging, more than Huntington disease, impairs the ubiquitin-proteasome system (UPS) for clearing toxic proteins.

Area of Science:

  • Cellular Biology
  • Neuroscience
  • Biochemistry

Background:

  • Cellular protein degradation is crucial for removing misfolded or damaged proteins, preventing toxicity.
  • Eukaryotic cells utilize the ubiquitin-proteasome system (UPS) and autophagy-lysosome pathways for protein clearance.
  • The UPS is present in the nucleus, suggesting its importance in clearing nuclear misfolded proteins, particularly relevant in neurodegenerative diseases.

Purpose of the Study:

  • To review the relationship between the ubiquitin-proteasome system (UPS) function, aging, and Huntington disease (HD).
  • To investigate the impact of aging and HD on the neuronal UPS capacity to clear toxic and misfolded proteins.
  • To highlight the role of aging as a significant factor negatively affecting UPS function.

Main Methods:

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Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein
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Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein

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Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
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Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

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Related Experiment Videos

Last Updated: Jun 6, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
07:08

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein
10:25

Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein

Published on: November 10, 2012

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

  • Literature review focusing on studies examining UPS function in aging and Huntington disease.
  • Analysis of existing research on protein degradation pathways in the context of neurodegeneration.
  • Synthesis of findings related to the selective neuropathology in HD and protein accumulation.

Main Results:

  • The ubiquitin-proteasome system (UPS) is critical for clearing misfolded proteins, including those implicated in Huntington disease (HD).
  • Aging appears to be a more significant factor than HD itself in negatively impacting the functional capacity of the neuronal UPS.
  • Misfolded proteins, characteristic of HD, accumulate in the nucleus, underscoring the UPS's nuclear role.

Conclusions:

  • The ubiquitin-proteasome system (UPS) plays a key role in cellular protein quality control, especially in the nucleus.
  • Aging significantly impairs UPS function, potentially exacerbating the effects of neurodegenerative diseases like Huntington disease.
  • Understanding the interplay between aging and the UPS is crucial for developing therapeutic strategies for proteinopathies.