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Updated: Jul 9, 2026
06:06
In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
Ubiquitin domain proteins in disease
Louise Madsen1, Andrea Schulze, Michael Seeger
1Insitute of Molecular Biology and Physiology, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen, Denmark.
BMC Biochemistry
|December 6, 2007
Summary
Ubiquitin-like domain proteins (UDPs) are crucial for cellular functions and protein degradation. Their diverse roles are linked to diseases like cancer and neurodegeneration.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- The human genome encodes multiple ubiquitin-like (UBL) domain proteins (UDPs).
- These proteins are integral to various cellular processes and the ubiquitin-proteasome system.
- UDPs exhibit functional diversity despite structural similarities.
Purpose of the Study:
- To summarize the biochemical and physiological roles of UDPs.
- To highlight the connection between UDPs and human diseases.
- To provide an overview of UDPs for researchers.
Main Methods:
- Literature review and data compilation from existing databases.
- Analysis of biochemical and physiological functions of UDPs.
- Correlation of UDP functions with disease pathologies.
Main Results:
- UDPs participate in a wide array of cellular functions.
- The ubiquitin-proteasome system heavily involves UDPs.
- UDP dysregulation is implicated in neurodegenerative disorders and cancer.
Conclusions:
- UDPs are a functionally diverse protein family with significant implications in human health.
- Understanding UDPs is critical for developing therapeutic strategies for associated diseases.
- Further research into UDPs will elucidate their precise roles in cellular mechanisms and disease pathogenesis.
Related Concept Videos
01:13The 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...
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...
02:18The 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...
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...
02:18The 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...
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...
02:04Covalently 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.
These groups modify specific amino acids in a protein.
02:58Regulated 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...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
02:58Regulated 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...
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