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Related Concept Videos

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.
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...
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...
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...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

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Related Experiment Video

Updated: May 21, 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 and its binding domains.

Leah Randles1, Kylie J Walters

  • 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

Frontiers in Bioscience (Landmark Edition)
|June 2, 2012
PubMed
Summary
This summary is machine-generated.

Ubiquitin modification is crucial for cell signaling and homeostasis. This study explores diverse ubiquitin receptors and their structural interactions, expanding our understanding of ubiquitin trafficking.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Post-translational modification by ubiquitin (ubiquitination) is a key signaling mechanism for cell homeostasis.
  • Ubiquitin signaling specificity relies on ubiquitin dynamics, chain multivalency, and subcellular context, involving ubiquitin receptors.
  • Over 150 ubiquitin receptors are known, featuring diverse ubiquitin-binding domains (UBDs).

Purpose of the Study:

  • To highlight various ubiquitin receptors with multiple UBD folds.
  • To focus on the structural characteristics of ubiquitin receptor-ubiquitin interactions.
  • To expand the ubiquitin-signaling map with newly identified UBD structural motifs.

Main Methods:

  • Literature review of identified ubiquitin receptors.
  • Structural analysis of diverse ubiquitin-binding domains (UBDs).
  • Focus on the interaction interfaces between UBDs and ubiquitin.

Main Results:

  • Ubiquitin receptors possess structurally diverse UBDs, including alpha-helical motifs, zinc fingers, PH domains, Ubc-related structures, and SH3 domains.
  • New UBD structural motifs are continuously identified.
  • These findings expand the known proteins and structural families involved in ubiquitin trafficking.

Conclusions:

  • Ubiquitin receptors play a critical role in mediating ubiquitin signaling specificity.
  • The structural diversity of UBDs contributes to the complexity of ubiquitin interactions.
  • Continued identification of novel UBDs broadens the scope of ubiquitin biology.