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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 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 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...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

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Related Experiment Video

Updated: May 12, 2026

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

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

Published on: December 17, 2016

The proteasome: from basic mechanisms to emerging roles.

Keiji Tanaka1

  • 1Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan. tanaka-kj@igakuken.or.jp

The Keio Journal of Medicine
|April 9, 2013
PubMed
Summary
This summary is machine-generated.

The proteasome

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Last Updated: May 12, 2026

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The proteasome is a large protein complex responsible for protein degradation within cells.
  • It comprises a catalytic core particle and regulatory particles.
  • Its precise assembly and function in immunity and disease are areas of active research.

Purpose of the Study:

  • To elucidate the assembly mechanism of the proteasome.
  • To identify and characterize novel proteasome isoforms.
  • To explore the proteasome's role in immunity and age-related diseases.

Main Methods:

  • Proposed a novel chaperone-assisted assembly mechanism.
  • Discovered and characterized two immuno-type proteasomes: immunoproteasome and thymoproteasome.
  • Reviewed emerging evidence on proteasome involvement in disease pathophysiology.

Main Results:

  • A novel proteasome assembly mechanism involving dedicated chaperones was proposed.
  • Two new proteasome isoforms, immunoproteasome and thymoproteasome, with specialized immune functions were identified.
  • The proteasome's critical role in the pathology of aging-related diseases is increasingly recognized.

Conclusions:

  • The proteasome's complex structure is organized with high fidelity through chaperone assistance.
  • Immuno-type proteasomes play specialized roles in cell-mediated immunity.
  • The proteasome is a significant factor in the pathophysiology of aging-associated diseases.