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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: May 24, 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 and function of the proteasome.

Yasushi Saeki1, Keiji Tanaka

  • 1Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.

Methods in Molecular Biology (Clifton, N.J.)
|February 22, 2012
PubMed
Summary
This summary is machine-generated.

The proteasome, a key cellular machine for protein degradation, is detailed in this review. It covers the structure, function, and assembly of the 26S proteasome, including its regulatory and core particles.

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Related Experiment Videos

Last Updated: May 24, 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:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The proteasome is a large protease complex essential for regulated protein degradation.
  • It comprises a 20S catalytic core particle (CP) and two 19S regulatory particles (RP), forming the 26S proteasome.
  • This complex degrades ubiquitylated proteins via recognition, unfolding, and translocation.

Purpose of the Study:

  • To review recent advancements in understanding the proteasome.
  • To summarize new insights into proteasome structure, function, and assembly.
  • To highlight the role of proteasome-dedicated chaperones.

Main Methods:

  • Literature review of recent scientific studies.
  • Synthesis of current knowledge on proteasome structure and function.
  • Analysis of proteasome assembly pathways.

Main Results:

  • Recent studies have elucidated complex functions of the 26S proteasome.
  • Identification of proteasome-dedicated chaperones reveals multistep assembly pathways for RP and CP.
  • Advances in understanding proteasome structure and its role in protein homeostasis.

Conclusions:

  • The proteasome is a dynamic and complex machine crucial for cellular protein turnover.
  • Understanding proteasome assembly is key to comprehending its overall function.
  • Continued research promises deeper insights into proteasome biology and therapeutic potential.