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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...
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...
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...

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Related Experiment Video

Updated: Jul 8, 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

Subunit-subunit interactions in the human 26S proteasome.

Chuan Chen1, Caoxin Huang, Shouhui Chen

  • 1Key Laboratory for Cell Biology and Tumor Cell Engineering, the Ministry of Education, School of Life Sciences, Xiamen University, Xiamen, China.

Proteomics
|January 11, 2008
PubMed
Summary

Researchers mapped interactions within the human 26S proteasome, identifying novel subunit connections. This work proposes a revised model for the proteasome

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Analyzing Large Protein Complexes by Structural Mass Spectrometry

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Last Updated: Jul 8, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Published on: December 17, 2016

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Published on: May 21, 2019

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ubiquitin-dependent proteolysis is a crucial cellular process regulated by the proteasome.
  • The human 26S proteasome is a large protein complex essential for protein degradation.
  • Understanding its structure and subunit interactions is key to elucidating its function.

Purpose of the Study:

  • To investigate the structural organization and functional interactions of human 26S proteasome subunits.
  • To identify novel protein-protein interactions within the human 26S proteasome complex.

Main Methods:

  • Cloning of complete open reading frames (ORFs) for 32 human proteasome subunits.
  • Yeast two-hybrid analysis to screen for subunit interactions.
  • GST-pull down assays to validate observed interactions.

Main Results:

  • Identified 114 interacting pairs among human 26S proteasome subunits.
  • Validated 10% (11/114) of these interactions using GST-pull down assays.
  • Discovered that 58% (66/114) of the observed interactions are novel, with 42% (48/114) previously reported.

Conclusions:

  • New interactions were found between the 19S regulatory particle and the beta-rings of the 20S catalytic core.
  • These findings support a modified model of the human 26S proteasome structure and assembly.
  • The study provides a comprehensive interaction map of the human 26S proteasome.