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Related Concept Videos

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...
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...
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...

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Related Experiment Video

Updated: Jun 15, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Multitasking with ubiquitin through multivalent interactions.

Fen Liu1, Kylie J Walters

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

Trends in Biochemical Sciences
|February 26, 2010
PubMed
Summary
This summary is machine-generated.

Ubiquitylation, a key protein modification, uses multivalency for specific cellular signaling. This involves multiple interaction surfaces across the ubiquitin pathway, ensuring precise regulation of cellular events.

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Last Updated: Jun 15, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
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Published on: May 14, 2021

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Biochemistry

Background:

  • Ubiquitylation is a crucial post-translational modification regulating diverse cellular processes in eukaryotes.
  • This modification involves the attachment of ubiquitin to proteins, influencing their function, localization, and degradation.
  • Existing knowledge highlights the versatility of ubiquitylation in controlling gene transcription and protein stability.

Purpose of the Study:

  • To elucidate the mechanisms underlying the specificity and versatility of ubiquitin signaling pathways.
  • To investigate the role of multivalency in regulating various stages of ubiquitin-mediated cellular events.
  • To identify the components within the ubiquitin system that utilize multivalent interactions.

Main Methods:

  • Analysis of protein-ubiquitin interactions.
  • Investigation of ubiquitin processing enzymes.
  • Characterization of ubiquitin recognition proteins.

Main Results:

  • Ubiquitylation employs multivalency, utilizing multiple interaction surfaces for precise cellular control.
  • Multivalent interactions are integral to the ubiquitin signal, ubiquitylated substrates, and associated enzymes.
  • These interactions are observed in ubiquitin recognition proteins, underscoring their widespread role.

Conclusions:

  • Multivalency is a fundamental principle enabling both versatility and specificity in ubiquitylation.
  • Coordinated use of multiple interaction surfaces ensures accurate signaling throughout the ubiquitylation pathway.
  • Understanding these multivalent interactions is key to deciphering complex cellular regulation.