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Related Concept Videos

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 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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jun 13, 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

Assembly, structure, and function of the 26S proteasome.

Lynn Bedford1, Simon Paine, Paul W Sheppard

  • 1School of Biomedical Sciences, University of Nottingham Medical School, Nottingham, UK.

Trends in Cell Biology
|April 30, 2010
PubMed
Summary

The 26S proteasome, crucial for protein degradation and cellular functions, is better understood with new insights into its assembly and structure. Malfunctions in this system are linked to disease pathogenesis.

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Related Experiment Videos

Last Updated: Jun 13, 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

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

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The 26S proteasome is a vital multiprotein complex regulating ubiquitinated protein degradation.
  • It controls essential cellular processes like DNA synthesis, repair, transcription, translation, and signal transduction.
  • Dysfunction of the ubiquitin proteasome system is implicated in various diseases.

Purpose of the Study:

  • To provide mechanistic insight into the assembly of the 26S proteasome.
  • To enhance the understanding of the proteasome's structure and function.
  • To elucidate the role of molecular chaperones in proteasome biogenesis.

Main Methods:

  • Identification of molecular chaperones involved in proteasome assembly.
  • Structural and functional analysis of the proteasome complex.
  • Investigation of the ubiquitin proteasome system's role in cellular mechanisms.

Main Results:

  • Four new molecular chaperones were identified, adding to five previously known ones.
  • These chaperones provide mechanistic insights into the assembly of the 26S proteasome.
  • New data offer a comprehensive understanding of the proteasome's structure and function.

Conclusions:

  • The identification of additional chaperones significantly advances our understanding of 26S proteasome assembly.
  • Enhanced knowledge of proteasome structure and function improves our grasp of its cellular roles.
  • This research deepens the understanding of a complex protease critical to cellular health and disease.