Related Experiment Video
Updated: Aug 19, 2025
06:06
In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
5.3K
Thioester and Oxyester Linkages in the Ubiquitin System
Alba Ferri-Blazquez1,2, Ernst Jarosch3, Thomas Sommer3,4
1Max-Delbrück-Center for Molecular Medicine in the Helmholz Association, Berlin Buch, Germany. albamaria.ferriblazquez@mdc-berlin.de.
Methods in Molecular Biology (Clifton, N.J.)
|November 29, 2022
Summary
Ubiquitylation typically involves covalent bonds, but new research reveals ester linkages to amino acids like cysteine. This expands the ubiquitin code, though its full role needs further study.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Signaling
Background:
- Traditional ubiquitylation involves covalent linkage of ubiquitin to lysine or N-terminal methionine residues.
- Emerging evidence shows ubiquitin can attach via ester bonds to amino acids like cysteine, serine, and threonine.
- Ester-linked ubiquitylation, initially observed in viral systems, is now recognized in cellular processes.
Approach:
- This review summarizes current knowledge on ester-linked ubiquitylation.
- It highlights experimental strategies to overcome analytical challenges.
- Focuses on understanding the prevalence and function of this modification.
Key Points:
- Ester-linked ubiquitylation represents a significant expansion of ubiquitin signaling diversity.
- This modification can involve cysteine residues, as seen in viral protein degradation.
- The precise physiological relevance and prevalence of ester-linked ubiquitylation are still under investigation.
Conclusions:
- Ester-linked ubiquitylation adds complexity to the ubiquitin code.
- Further research is needed to elucidate its roles in cellular functions and disease.
- Developing robust analytical methods is crucial for studying this posttranslational modification.
Related Concept Videos
01:13The Proteasome
1.0K
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...
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...
1.0K
01:26Protein Modifications in the RER
5.4K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.4K
02:04Covalently Linked Protein Regulators
6.9K
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....
6.9K
01:17The Proteasome Structure
858
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...
The proteasome is an...
858
02:58Regulated Protein Degradation
7.5K
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...
7.5K
01:01Phosphodiester Linkages
101.8K
Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
101.8K