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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...
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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.

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Correction: Prasad et al. Patterns of Variation in the Usage of Fatty Acid Chains among Classes of Ester and Ether Neutral Lipids and Phospholipids in the Queensland Fruit Fly. <i>Insects</i> 2023, <i>14</i>, 873.

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Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples
09:45

Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples

Published on: May 10, 2015

Deubiquitylating enzymes and disease.

Shweta Singhal1, Matthew C Taylor, Rohan T Baker

  • 1Ubiquitin Laboratory, Division of Molecular Bioscience, The John Curtin School of Medical Research, The Australian National University, Canberra, ACT 0200, Australia. Shweta.Singhal@anu.edu.au

BMC Biochemistry
|November 26, 2008
PubMed
Summary

Deubiquitylating enzymes (DUBs) remove ubiquitin from proteins, regulating cellular processes like proteolysis and trafficking. Many DUBs are implicated in diseases, offering potential therapeutic targets.

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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay

Published on: September 27, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Deubiquitylating enzymes (DUBs) are crucial for reversing ubiquitination, a key post-translational modification.
  • DUBs regulate essential cellular functions, including protein degradation and trafficking.
  • Mammals possess a large family of DUBs, with most remaining uncharacterized.

Purpose of the Study:

  • To review the role of DUBs in cellular processes and disease.
  • To highlight the therapeutic potential of targeting DUBs.

Main Methods:

  • Literature review and data compilation from the Targeted Proteins database (TPdb).
  • Analysis of DUB interactions and functions.
  • Examination of DUBs' involvement in various pathologies.

Main Results:

  • DUBs hydrolyze various bonds to remove ubiquitin, impacting cellular pathways.
  • Approximately 80-90 DUBs exist in mammals, categorized into five subfamilies.
  • Numerous DUBs are linked to diseases through mutations, altered expression, or regulatory complex formation.

Conclusions:

  • DUBs are critical regulators of ubiquitylation-mediated cellular events.
  • Dysregulation of DUBs is associated with diverse diseases, presenting therapeutic opportunities.
  • Despite no current drugs, accumulated data supports the rapid development of DUB-targeting therapies.