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Related Concept Videos

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...
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...
Regulated Protein Degradation02:58

Regulated Protein Degradation

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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...

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Related Experiment Video

Updated: Jun 14, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Ubiquitin chain cleavage: CYLD at work.

Ramin Massoumi1

  • 1Department of Laboratory Medicine, Clinical Research Center, Lund University, SE-205 Malmö, Sweden. Ramin.Massoumi@med.lu.se

Trends in Biochemical Sciences
|March 30, 2010
PubMed
Summary

The tumor suppressor CYLD, a deubiquitylating enzyme, negatively regulates cell signaling pathways. Its loss, through mutation or epigenetic changes, can promote tumor growth and inflammation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • CYLD is a deubiquitylating enzyme that negatively regulates signaling pathways.
  • Loss of CYLD expression is implicated in various tumor types, promoting cell survival and proliferation.
  • CYLD regulation occurs via mutations, transcriptional/post-transcriptional mechanisms, and epigenetic repression.

Purpose of the Study:

  • To elucidate the multifaceted regulatory mechanisms governing CYLD activity.
  • To understand the role of CYLD in controlling inflammatory responses and tumor progression.

Main Methods:

  • Analysis of CYLD's deubiquitylating enzyme activity.
  • Investigation of transcriptional and post-transcriptional regulation of CYLD.
  • Assessment of epigenetic control over the CYLD promoter.

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Ubiquitin Chain Analysis by Parallel Reaction Monitoring
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Ubiquitin Chain Analysis by Parallel Reaction Monitoring

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In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
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In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

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Related Experiment Videos

Last Updated: Jun 14, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

  • Study of post-translational modifications, such as phosphorylation, affecting CYLD.

    • Main Results:

    • CYLD removes lysine 63-linked polyubiquitin chains from specific substrates.
    • Epigenetic repression of CYLD impacts tumor progression and inflammatory response.
    • CYLD activity is further modulated by regulatory mechanisms like phosphorylation.

    Conclusions:

    • CYLD acts as a critical tumor suppressor through deubiquitylation.
    • Tight control of CYLD expression and activity is essential for regulating inflammatory responses and preventing tumorigenesis.
    • Multiple regulatory layers ensure precise control over CYLD's physiological functions.