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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

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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

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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Related Experiment Video

Updated: Feb 11, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Structure and Function of the 26S Proteasome.

Jared A M Bard1,2, Ellen A Goodall1,2, Eric R Greene1,2

  • 1Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA;

Annual Review of Biochemistry
|April 14, 2018
PubMed
Summary

The 26S proteasome, a key protein degradation machine, uses complex mechanisms for substrate selection and processing. Recent studies reveal its intricate conformational landscape, crucial for regulating cellular protein levels.

Keywords:
26S proteasomeAAA+ ATPasedeubiquitinationenergy-dependent protein degradationubiquitin codeubiquitin receptor

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The 26S proteasome is central to the ubiquitin-proteasome system, degrading proteins in eukaryotic cells.
  • It regulates critical cellular processes including homeostasis, stress response, cell division, and signal transduction.

Purpose of the Study:

  • To elucidate the mechanisms of substrate processing by the 26S proteasome.
  • To understand how the proteasome achieves both broad substrate recognition and high selectivity.

Main Methods:

  • Utilized recent structural and biochemical studies.
  • Investigated proteasomal substrate recognition, deubiquitination, and translocation.
  • Analyzed the conformational landscape of the proteasome.

Main Results:

  • Identified key steps in proteasomal substrate processing: recognition, deubiquitination, and ATP-driven unfolding/translocation.
  • Revealed a complex conformational landscape that governs substrate selection.
  • Demonstrated the proteasome's ability to balance promiscuity with selectivity.

Conclusions:

  • Advances in understanding the 26S proteasome's machinery have been made.
  • The proteasome's conformational dynamics are critical for its regulatory functions.
  • This knowledge provides a foundation for future research on proteasome-mediated proteome regulation.