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Related Concept Videos

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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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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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.
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Cracking the Ubiquitin Code: The Ubiquitin Toolbox.

Monique P C Mulder1, Katharina F Witting1, Huib Ovaa1

  • 1Oncode Institute and Department of Cell and Chemical Biology, Chemical Immunology, Leiden University Medical Centre, Leiden, the Netherlands.

Current Issues in Molecular Biology
|November 2, 2019
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Ubiquitination regulates cellular processes, and its enzymes are key in diseases like cancer. New tools, including activity-based probes, are crucial for studying these enzymes and developing therapeutics.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Drug Discovery

Background:

  • Ubiquitination is a critical post-translational modification regulating numerous cellular processes.
  • Dysregulation of ubiquitination enzymes is implicated in major pathologies, including cancer and neurodegenerative diseases.
  • Understanding the ubiquitination cascade, involving enzyme activation, conjugation, ligation, and deubiquitination, is vital for cellular homeostasis.

Purpose of the Study:

  • To review the current landscape of tools for studying ubiquitination.
  • To highlight the importance of developing novel reagents and technologies for ubiquitin research.
  • To underscore the significance of identifying inhibitors for ubiquitin-modifying enzymes.

Main Methods:

  • Review of synthetic strategies for ubiquitin generation.
  • Analysis of existing ubiquitin assay reagents and activity-based probes (ABPs).
  • Examination of reporter substrates and other Ub-based recognition tools.

Main Results:

  • Advances in synthetic ubiquitin chemistry have enabled the development of diverse assay reagents and ABPs.
  • Current tools facilitate the study of enzymes within the complex ubiquitination system.
  • The chapter showcases state-of-the-art ABPs and reporter substrates.

Conclusions:

  • Innovative tools are essential for dissecting complex ubiquitin biology.
  • Developing ABPs and high-throughput assay reagents is paramount for identifying therapeutic targets.
  • Further technological advancements are needed to explore emerging aspects of ubiquitin regulation and its role in disease.