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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....

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Related Experiment Video

Updated: Jun 7, 2025

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Decoding Ubiquitin Modifications by Mass Spectrometry.

Yanqiu Gong¹, Lunzhi Dai²

¹National Clinical Research Center for Geriatrics and Department of General Practice, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.

Advances in Experimental Medicine and Biology

|November 15, 2024

Summary

Protein ubiquitination, a key cellular regulator, is decoded using mass spectrometry (MS)-based proteomics. This approach reveals complex ubiquitin chains and their roles in cellular processes like DNA repair and immunity.

Keywords:

Lysine ubiquitinome Post-translational modification Tandem mass spectrometry

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Last Updated: Jun 7, 2025

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Area of Science:

Biochemistry
Molecular Biology
Cellular Biology

Background:

Protein ubiquitination is a crucial post-translational modification regulating diverse cellular functions.
Understanding ubiquitin networks is vital for deciphering cellular processes such as proteostasis, DNA repair, trafficking, and immunity.

Purpose of the Study:

To discuss the application of mass spectrometry (MS) in interpreting the ubiquitin code.
To highlight how MS-based proteomics decodes the complexity of ubiquitin networks.

Main Methods:

Mass spectrometry (MS)-based proteomics is employed to analyze ubiquitination.
This technique identifies ubiquitination sites across the proteome.
MS enables the characterization of ubiquitin chain length, linkage, and topology.

Main Results:

MS-based proteomics provides a comprehensive view of ubiquitination.
The method can reveal modifications on ubiquitin chains.
It also uncovers crosstalk between ubiquitination and other post-translational modifications.

Conclusions:

Mass spectrometry is a powerful tool for understanding the ubiquitin code.
Deciphering ubiquitination networks through MS enhances our knowledge of cellular regulation.
This approach is essential for studying complex biological pathways.