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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

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Reporter-based Growth Assay for Systematic Analysis of Protein Degradation
07:47

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Published on: November 6, 2014

Stressing the ubiquitin-proteasome system.

Nico P Dantuma1, Kristina Lindsten

  • 1Department of Cell and Molecular Biology, Karolinska Institutet, von Eulers väg 3 S-17177, Stockholm, Sweden. nico.dantuma@ki.se

Cardiovascular Research
|July 28, 2009
PubMed
Summary
This summary is machine-generated.

Cells must eliminate toxic unfolded and misfolded proteins. Proteotoxic stress can impair the ubiquitin-proteasome system (UPS), leading to cell dysfunction and disease.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Unfolded and misfolded proteins pose a significant threat to cellular health.
  • Elevated levels of misfolded proteins occur during proteotoxic stress.
  • Metazoan cells possess protein quality control mechanisms to manage non-native proteins.

Purpose of the Study:

  • To review the current understanding of proteotoxic stress-induced dysfunction of the ubiquitin-proteasome system (UPS).
  • To explore the implications of UPS dysfunction in human pathologies.

Main Methods:

  • This review synthesizes findings from existing studies on proteotoxic stress and UPS function.
  • Literature review focusing on cellular responses to misfolded proteins and UPS impairment.

Main Results:

  • Proteotoxic stress conditions can lead to functional impairment of the UPS.
  • Impaired UPS function results in cellular dysfunction and apoptosis.
  • The UPS is a critical defense mechanism for eliminating toxic proteins.

Conclusions:

  • Understanding proteotoxic stress-induced UPS dysfunction is crucial for comprehending human diseases.
  • Targeting the UPS may offer therapeutic strategies for pathologies associated with protein misfolding.