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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...
The Effect of Aging on Tissues01:19

The Effect of Aging on Tissues

Several body functions deteriorate with age. The external signs of aging are easily identifiable. For example, the skin becomes dry, less elastic, and thins out, forming wrinkles. The skin of the face begins to appear looser due to a decrease in the levels of elastic and collagen fibers in the connective tissue. Additionally, melanin production in the hair follicle decreases with age, resulting in gray hair. Moreover, the senses of sight and hearing decline, so glasses and hearing aids may...
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: May 21, 2026

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

Changes of the proteasomal system during the aging process.

Martin A Baraibar1, Bertrand Friguet

  • 1Laboratoire de Biologie Cellulaire du Vieillissement, UR4-IFR83, Université Pierre et Marie Curie–Paris 6, 4 place Jussieu, Paris Cedex 05, France.

Progress in Molecular Biology and Translational Science
|June 26, 2012
PubMed
Summary
This summary is machine-generated.

Protein accumulation damages cells during aging. The proteasomal system, crucial for protein quality control, declines with age, potentially driving aging and related diseases. Rejuvenating proteasome function may offer anti-aging benefits.

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Assessing Lysosomal Alkalinization in the Intestine of Live Caenorhabditis elegans

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Related Experiment Videos

Last Updated: May 21, 2026

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

Assessing Lysosomal Alkalinization in the Intestine of Live Caenorhabditis elegans
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Assessing Lysosomal Alkalinization in the Intestine of Live Caenorhabditis elegans

Published on: April 13, 2018

Area of Science:

  • Biogerontology
  • Molecular Biology
  • Cellular Homeostasis

Background:

  • Accumulation of damaged proteins is a key feature of aging.
  • Intracellular protein degradation prevents protein toxicity and preserves amino acid reserves.
  • The proteasomal system is vital for maintaining cellular protein homeostasis.

Purpose of the Study:

  • To review the age-related changes in proteasome function across various biological levels.
  • To explore the molecular mechanisms underlying the decline in proteasome activity during aging.
  • To discuss interventions targeting proteasome function as potential anti-aging strategies.

Main Methods:

  • Review of existing literature on proteasome function in aging.
  • Analysis of molecular mechanisms contributing to age-related proteasome decline.
  • Discussion of therapeutic interventions for proteasome rejuvenation.

Main Results:

  • Proteasome function is demonstrably impaired in aging organs, tissues, cells, and model organisms.
  • Evidence suggests a causal link between reduced proteasome activity and the aging process.
  • Age-associated diseases may be linked to this decline in proteasome function.

Conclusions:

  • Impaired proteasome function is a significant factor in aging.
  • Understanding the molecular basis of this decline is crucial for developing anti-aging strategies.
  • Targeting proteasome rejuvenation holds promise for combating age-related decline and diseases.