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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 Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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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Related Experiment Video

Updated: Jun 6, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

Luisa M Napolitano1, Ellis G Jaffray, Ronald T Hay

  • 1Cluster in Biomedicine (CBM), AREA Science Park, s.s. 14 km 163.5 Basovizza, 34149 Trieste, Italy.

The Biochemical Journal
|December 15, 2010
PubMed
Summary

This study screened interactions between TRIM and UBE2 proteins, revealing specific pairings like TRIM9 with UBE2G2. These TRIM-UBE2 interactions are crucial for TRIM E3 ligase activity and cellular function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • The TRIM (tripartite motif) family comprises the largest subfamily of RING-finger E3 ubiquitin ligases.
  • TRIM proteins are implicated in diverse cellular processes, but their specific E2 enzyme interactions remain largely uncharacterized.

Purpose of the Study:

  • To comprehensively screen interactions between the TRIM and UBE2 enzyme families.
  • To elucidate the specificity and physiological relevance of TRIM-UBE2 enzyme complex formation.

Main Methods:

  • Systematic screening of TRIM-UBE2 interactions.
  • Analysis of E3 ligase activity dependent on specific UBE2 partners.
  • Subcellular co-localization studies of TRIM and UBE2 proteins.

Main Results:

  • TRIM proteins generally favor UBE2 enzymes of classes D and E.
  • Highly specific interactions were identified, including TRIM9-UBE2G2 and TRIM32-UBE2V1/2.
  • TRIM E3 ligase activity is contingent upon interaction with specific UBE2 enzymes.
  • Co-localization of interacting TRIM-UBE2 pairs suggests physiological significance.

Conclusions:

  • TRIM-UBE2 interactions are specific and essential for TRIM E3 ligase function.
  • The identified specific TRIM-UBE2 pairs provide a foundation for studying their roles in targeted protein ubiquitination.
  • Further research into these specific complexes will clarify their roles in determining target protein fate.