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Related Concept Videos

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 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 Proteasome Structure01:17

The Proteasome Structure

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...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

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Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

ASK1 negatively regulates the 26 S proteasome.

Ji Won Um1, Eunju Im, Joongkyu Park

  • 1Department of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.

The Journal of Biological Chemistry
|September 17, 2010
PubMed
Summary

Apoptosis signal-regulating kinase 1 (ASK1) inhibits 26 S proteasome activity by phosphorylating Rpt5, a key ATPase. This discovery reveals a novel regulatory mechanism for proteasome function and disease treatment.

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Last Updated: Jun 8, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
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Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

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Published on: December 17, 2016

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The 26 S proteasome is crucial for protein degradation via ubiquitination.
  • Dysregulation of proteasome activity is implicated in various diseases.
  • Mechanisms controlling 26 S proteasome activity are not fully understood.

Purpose of the Study:

  • To investigate the role of apoptosis signal-regulating kinase 1 (ASK1) in regulating 26 S proteasome activity.
  • To elucidate the molecular mechanisms by which ASK1 affects proteasome function.

Main Methods:

  • Cell culture experiments
  • In vitro assays
  • Immunoprecipitation and Western blot analyses
  • Enzyme activity assays

Main Results:

  • ASK1 negatively regulates 26 S proteasome activity.
  • ASK1 interacts with ATPases of the 19 S regulatory particle, not the 20 S core.
  • ASK1 phosphorylates Rpt5, inhibiting its ATPase activity, thereby reducing 26 S proteasome function.

Conclusions:

  • ASK1 plays a novel role in the regulation of 26 S proteasome activity.
  • The findings suggest potential therapeutic strategies for diseases linked to proteasome malfunction.