Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Covalently Linked Protein Regulators

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....

You might also read

Related Articles

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

Sort by

Same author

Disentangling the response to lysosomal damage.

Journal of cell science·2026

Same author

Targeted degradation of USP7 in solid cancer cells reveals distinct effects of deubiquitinase degraders and inhibitors.

Nature communications·2026

Same author

HM-DyadCap - capture and mapping of 5-hydroxymethylcytosine/5-methylcytosine CpG dyads in mammalian DNA.

Nucleic acids research·2026

Same author

Unraveling Synthetase's Mode of Action: The Pyrrolysyl-tRNA Synthetase Dimer Uses Secondary Binding Sites in the Cell.

Angewandte Chemie (International ed. in English)·2026

Same author

The accessory adapters FAF1, FAF2, and UBXN7 accelerate proteasomal degradation by increasing prior p97-mediated substrate unfolding.

Science advances·2026

Same author

The role of cytosine modification symmetry in mammalian epigenome regulation.

Chemical science·2026

Search research articles

Related Experiment Video

Updated: Jun 4, 2025

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Light-Activatable Ubiquitin for Studying Linkage-Specific Ubiquitin Chain Formation Kinetics.

Sudakshina Banerjee¹, Zeyneb Vildan Cakil¹, Kai Gallant^1,2

¹Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn Str. 4a, 44227, Dortmund, Germany.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)

|December 24, 2024

Summary

Researchers developed a new method to study ubiquitination dynamics using light-activated ubiquitin chains. This technique allows for precise monitoring of linkage-specific ubiquitination kinetics in real-time.

Keywords:

genetic code expansion optochemical biology small molecule inhibitors ubiquitin

More Related Videos

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Related Experiment Videos

Last Updated: Jun 4, 2025

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Ubiquitination is a crucial post-translational modification regulating protein fate.
Ubiquitin chains feature diverse linkage types, creating a complex regulatory code.
Studying the dynamics of specific ubiquitin linkages remains challenging.

Purpose of the Study:

To develop a method for light-dependent, linkage-specific polyubiquitin chain formation.
To enable real-time monitoring of ubiquitination kinetics.
To investigate the role of the ubiquitin-proteasome system in chain synthesis.

Main Methods:

Incorporation of photocaged lysine into ubiquitin via amber codon suppression.
Light-dependent activation of ubiquitin chain extension.
Small molecule inhibition to study ubiquitin-proteasome system components.

Main Results:

Demonstrated light-activatable polyubiquitin chain formation.
Revealed rapid, minute-scale ubiquitination kinetics for K11, K48, and K63 linkages.
Investigated the role of ubiquitin-proteasome system components in K48-chain synthesis.

Conclusions:

Developed a novel tool for temporal control of linkage-specific ubiquitination.
The method allows high-resolution studies of ubiquitinome dynamics.
Broad applications expected for dissecting ubiquitination pathways.