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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...
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...
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...
Antigen Processing Pathways01:31

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...

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Proteasomes generate spliced epitopes by two different mechanisms and as efficiently as non-spliced epitopes.

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Related Experiment Video

Updated: Jun 7, 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 27, 2014

Antigen processing by the proteasome.

P M Kloetzel1

  • 1Institut für Biochemie, Medical Faculty, Charité, Humboldt University, Monbijoustrasse 2, 10117 Berlin, Germany. p-m.kloetzel@charite.de

Nature Reviews. Molecular Cell Biology
|March 27, 2001
PubMed
Summary

The proteasome, a cellular waste disposal unit, adapts to efficiently generate peptides for immune surveillance. This adaptation is crucial for presenting antigens to T cells, enhancing immune response.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • The proteasome is vital for immune surveillance by processing intracellular antigens into peptides.
  • Typically, proteasomes generate these peptides inefficiently for T cell presentation.
  • Cellular proteasomes act as waste-disposal units, presenting a paradox in their immune function.

Purpose of the Study:

  • To investigate how proteasomes adapt to enhance peptide generation for immune surveillance.
  • To understand the mechanisms underlying the proteasome's dual role in cellular waste disposal and immune presentation.

Main Methods:

  • Analysis of proteasome activity under various cellular conditions.
  • Biochemical assays to quantify peptide generation efficiency.
  • Immunological studies to assess T cell recognition of proteasome-derived peptides.

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

Published on: December 17, 2016

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

Related Experiment Videos

Last Updated: Jun 7, 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 27, 2014

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

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

Main Results:

  • Proteasomes exhibit regulatory mechanisms that increase peptide generation efficiency for immune presentation.
  • Specific proteasome subunits or associated factors are involved in this adaptation.
  • Enhanced peptide presentation correlates with improved T cell activation.

Conclusions:

  • The proteasome dynamically adapts its function to optimize peptide generation for effective immune surveillance.
  • Understanding these adaptations offers insights into modulating immune responses.
  • Targeting proteasome adaptation could be a strategy for immune-based therapies.