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Related Concept Videos

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...
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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Related Experiment Video

Updated: Jun 5, 2026

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

Proteasome activators.

Beth M Stadtmueller1, Christopher P Hill

  • 1Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.

Molecular Cell
|January 8, 2011
PubMed
Summary
This summary is machine-generated.

Proteasome activators are crucial for protein degradation. This study provides a structural view of how proteasomes are activated and how substrates access their proteolytic sites, enhancing our understanding of cellular protein homeostasis.

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Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
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Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

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Last Updated: Jun 5, 2026

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07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

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05:33

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Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
10:44

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

Published on: May 15, 2019

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Proteasomes are essential cellular machines responsible for degrading proteins in the cytosol and nucleus.
  • Their proteolytic sites are sequestered, necessitating activators for substrate access.
  • Previous studies explored 11S and Blm10 activators, but the third activator family, including the 19S activator, remains less understood.

Purpose of the Study:

  • To provide a structural perspective on proteasome activation mechanisms.
  • To elucidate how substrates are delivered to the proteasome's proteolytic sites.
  • To enhance the understanding of the third activator family, specifically the 19S activator.

Main Methods:

  • Structural studies
  • Biochemical analyses

Main Results:

  • Insights into the mechanisms of proteasome activation by different activator families.
  • Structural understanding of substrate delivery pathways to the proteasome.
  • Clarification of the role of the 19S activator in targeting polyubiquitylated proteins.

Conclusions:

  • Proteasome activators are key to regulating protein degradation.
  • Structural insights are vital for understanding proteasome function and substrate processing.
  • Further research into activator families like the 19S activator is crucial for comprehending cellular protein turnover.