Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
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....
9.9K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
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...
3.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
2.2K
The Proteasome01:13

The Proteasome

2.0K
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...
2.0K
The Proteasome02:18

The Proteasome

10.5K
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...
10.5K
Regulated Protein Degradation02:58

Regulated Protein Degradation

9.2K
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...
9.2K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Systemic degradation of repressive transcription factors gates gene expression and cell fate specification.

bioRxiv : the preprint server for biology·2026
Same author

Localized heme sensing through a ternary molecular glue.

bioRxiv : the preprint server for biology·2026
Same author

Scalable longitudinal imaging and transcriptomics of cells in dynamic enclosures.

bioRxiv : the preprint server for biology·2026
Same author

The E3-ome gene-centric compendium reveals the human E3 ligase landscape.

Cell·2026
Same author

Function and regulation of the mitochondrial stress response.

Nature structural & molecular biology·2026
Same author

Poxvirus attack of antiviral defense pathways unleashes an effector-triggered NF-κB response.

Science (New York, N.Y.)·2026

Related Experiment Video

Updated: Mar 20, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

6.1K

The increasing complexity of the ubiquitin code.

Richard Yau1,2, Michael Rape1,2

  • 1Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.

Nature Cell Biology
|May 28, 2016
PubMed
Summary
This summary is machine-generated.

Ubiquitylation, a key cellular process, uses diverse ubiquitin chains to regulate signal transduction, cell division, and differentiation. Understanding novel chain types reveals how cells achieve precise and robust communication.

More Related Videos

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

4.1K
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

11.6K

Related Experiment Videos

Last Updated: Mar 20, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

6.1K
Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

4.1K
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

11.6K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ubiquitylation is a crucial post-translational modification regulating fundamental cellular processes.
  • Substrate ubiquitylation can involve single ubiquitin molecules or complex chains, leading to diverse cellular outcomes.
  • Recent discoveries of novel ubiquitin chain topologies are enhancing our comprehension of cellular signaling.

Purpose of the Study:

  • To discuss the role of increasing ubiquitylation complexity in eukaryotic cells.
  • To highlight how diverse ubiquitylation patterns ensure robust signal transduction.
  • To explore the implications of novel ubiquitin chain topologies for cellular communication.

Main Methods:

  • Literature review of recent advancements in ubiquitylation research.
  • Analysis of studies detailing novel ubiquitin chain topologies.
  • Discussion of the functional consequences of different ubiquitylation patterns.

Main Results:

  • Ubiquitylation encompasses a wide spectrum of modifications, from single ubiquitin to complex chains.
  • Novel ubiquitin chain topologies contribute to the specificity and fidelity of cellular signaling.
  • The complexity of ubiquitylation is integral to establishing precise intracellular communication networks.

Conclusions:

  • The intricate nature of ubiquitylation is essential for reliable signal transduction in eukaryotes.
  • Understanding diverse ubiquitylation mechanisms provides insights into cell division and differentiation.
  • Further research into ubiquitin chain topology will deepen our knowledge of cellular regulation.