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Updated: Feb 14, 2026
Detection of Protein Ubiquitination
Published on: August 19, 2009
Doxorubicin-induced DNA Damage Causes Extensive Ubiquitination of Ribosomal Proteins Associated with a Decrease in
Vincentius A Halim1, Iraia García-Santisteban2, Daniel O Warmerdam3
1Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CH Utrecht, The Netherlands; Netherlands Proteomics Centre, 3584 CH Utrecht, The Netherlands; Division of Cell Biology and Cancer Genomics Center, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands.
DNA double-strand breaks trigger widespread changes in protein ubiquitination, particularly affecting ribosomal proteins. This study reveals the ribosome as a key target in the DNA damage response, impacting its function.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Protein posttranslational modifications (PTMs) are crucial for cellular processes.
- Phosphorylation and ubiquitination are key PTMs in the DNA damage response (DDR).
- The DDR coordinates DNA break repair with cell cycle progression.
Purpose of the Study:
- To identify global changes in protein ubiquitination following DNA double-strand breaks using quantitative proteomics.
- To investigate the role of ubiquitination in the DNA damage response.
Main Methods:
- Whole-cell quantitative proteomics was employed.
- Over 9,400 ubiquitin sites were quantified.
- Changes in ubiquitin site abundance upon DNA damage induction were analyzed.
Main Results:
- Approximately 10% of quantified ubiquitin sites showed altered abundance after DNA double-strand breaks.
- A significant number of ribosomal proteins (40S and 60S subunits) were ubiquitinated in response to DNA damage.
- DNA damage was found to inhibit ribosome function.
Conclusions:
- The ribosome is a major target of the DNA damage response.
- Ubiquitination of ribosomal proteins is a key event in the DDR.
- DNA damage impacts ribosome function through PTMs.
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