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Related Experiment Video

Updated: May 7, 2026

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

Published on: May 17, 2016

USP10: friend and foe.

Aart G Jochemsen¹, Yosef Shiloh

¹Department of Molecular Cell Biology, Leiden University Medical Center, 2300RC Leiden, The Netherlands. a.g.jochemsen@lumc.nl

|February 11, 2010

Summary

Researchers discovered USP10, a deubiquitinating protease, regulates the tumor suppressor protein p53. This finding is crucial for understanding DNA damage response and tumor development.

Area of Science:

Molecular Biology
Cancer Research
Biochemistry

Background:

The tumor suppressor protein p53 is vital for the DNA damage response.
p53 activity is primarily regulated through ubiquitination.
Understanding p53 regulation is key to cancer development research.

Purpose of the Study:

To identify novel regulators of p53 in the DNA damage response.
To investigate the role of deubiquitinating proteases in p53 regulation.
To explore the implications of p53 regulation in tumor development.

Main Methods:

Investigated the interaction between USP10 and p53.
Assessed the impact of USP10 on p53 ubiquitination levels.
Examined the functional consequences of USP10-mediated p53 regulation in cellular models.

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Last Updated: May 7, 2026

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

Published on: May 17, 2016

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

HOX Loci Focused CRISPR/sgRNA Library Screening Identifying Critical CTCF Boundaries

HOX Loci Focused CRISPR/sgRNA Library Screening Identifying Critical CTCF Boundaries

Published on: March 31, 2019

Main Results:

Identified USP10 as a deubiquitinating protease that directly interacts with p53.
Demonstrated that USP10 deubiquitinates p53, affecting its stability and activity.
Showcased USP10's role in modulating the DNA damage response pathway through p53 regulation.

Conclusions:

USP10 is a newly identified regulator of the tumor suppressor protein p53.
USP10 influences the DNA damage response and has implications for tumor development.
Targeting USP10 may offer new therapeutic strategies for cancer treatment.