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Related Concept Videos

The Proteasome Structure01:17

The Proteasome Structure

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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...
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The Proteasome02:18

The Proteasome

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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.
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The Proteasome01:13

The Proteasome

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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.
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The Proteasome02:18

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Protein Complex Assembly02:41

Protein Complex Assembly

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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.
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Protein Complex Assembly02:41

Protein Complex Assembly

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Updated: Mar 1, 2026

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

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Proteasome Structure and Assembly.

Lauren Budenholzer1, Chin Leng Cheng1, Yanjie Li1

  • 1Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.

Journal of Molecular Biology
|June 7, 2017
PubMed
Summary
This summary is machine-generated.

The 26S proteasome, crucial for protein degradation, involves complex assembly. Recent cryo-electron microscopy studies reveal new details about its structure and dynamics, advancing our understanding of this vital cellular machine.

Keywords:
proteasomeproteasome assemblyprotein degradationubiquitin proteasome system

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Area of Science:

  • Cellular Biology
  • Molecular Machinery
  • Protein Degradation

Background:

  • The eukaryotic 26S proteasome is a large, multi-subunit complex essential for regulated protein degradation.
  • It comprises the 19S regulatory particle and the 20S core particle, with substrates typically ubiquitinated for recognition.
  • Proper assembly of this ~2.5 MDa complex is critical for cellular function.

Purpose of the Study:

  • To review recent advances in understanding proteasome assembly mechanisms.
  • To highlight the impact of new structural information on proteasome research.
  • To focus on the intricate orchestration of 26S proteasome formation.

Main Methods:

  • Review of recent scientific literature.
  • Analysis of atomic cryo-electron microscopy (cryo-EM) structures of human and yeast 26S proteasomes.
  • Integration of structural findings with knowledge of proteasome assembly pathways.

Main Results:

  • Significant progress has been made in elucidating proteasome assembly, structure, and function.
  • Atomic cryo-EM structures have revealed novel intricacies and dynamics of the 26S proteasome.
  • Recent structural data provides critical insights into the mechanisms governing proteasome assembly.

Conclusions:

  • The review synthesizes current knowledge on proteasome assembly, informed by cutting-edge structural biology.
  • Understanding proteasome assembly is crucial for comprehending its role in cellular protein homeostasis.
  • Advances in cryo-EM continue to drive discoveries in the field of proteasome research.