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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....

Regulated Protein Degradation

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...

Receptor Downregulation in MVBs

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...

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Related Experiment Video

Updated: Apr 12, 2026

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

Quantifying ubiquitin signaling.

Alban Ordureau¹, Christian Münch¹, J Wade Harper¹

¹Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

|May 23, 2015

Summary

This summary is machine-generated.

Quantitative proteomics advances the study of ubiquitin (UB)-driven signaling pathways. These methods quantify UB modifications and their integration with phosphorylation, offering new insights into biological systems.

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Last Updated: Apr 12, 2026

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Published on: November 7, 2019

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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

Area of Science:

Biochemistry
Cell Biology
Proteomics

Background:

Ubiquitin (UB)-driven signaling pathways are crucial in biology, often interacting with other post-translational modifications (PTMs) like phosphorylation.
Understanding the dynamics and stoichiometry of intermediates in these pathways is challenging.
The spatial organization and fractional stoichiometry of pathway components regulate biological flux.

Purpose of the Study:

To review the application of quantitative proteomic tools for analyzing UB-dependent signaling systems.
To highlight the integration of UB signaling with regulatory phosphorylation events.
To discuss methods for identifying and quantifying UB chain synthesis and linkage preferences.

Main Methods:

Quantitative proteomic tools and enrichment strategies are employed.
Proteomic and enzymological approaches are used to analyze UB chain formation.
Case studies, such as the PINK1/PARKIN pathway, illustrate the methodologies.

Main Results:

Quantitative proteomics enables the measurement of UB-dependent signaling dynamics and stoichiometry.
These methods facilitate the integration of UB signaling with phosphorylation.
Identification and quantification of UB chain linkage types and synthesis are achievable.

Conclusions:

Sophisticated quantitative proteomic approaches are setting new standards for understanding UB-driven signaling.
These advancements are crucial for elucidating the biochemical mechanisms underlying complex cellular pathways.
A deeper comprehension of UB signaling dynamics and its interplay with other PTMs is emerging.