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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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Updated: Mar 15, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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Ubiquitin System-Driven Proteostasis in DNA Damage Response.

Renata Kusuma1,2, Audrey Regina Valerie1,2, Sisi Qin3

  • 1Department of Integrated Biomedical Science, Soonchunhyang Institute of Medi-bio-Science (SIMS), Soonchunhyang University, Cheonan 31151, Republic of Korea.

International Journal of Molecular Sciences
|March 14, 2026
PubMed
Summary

The ubiquitin system is crucial for maintaining proteostasis and regulating the DNA damage response (DDR). Targeting ubiquitin components offers potential therapeutic strategies for cancer by restoring DDR signaling.

Keywords:
DNA damage responsecancer therapygenomic instabilityproteostasisubiquitin-system

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Proteostasis, the maintenance of protein homeostasis, is vital for cellular function.
  • The ubiquitin system regulates protein stability, trafficking, and degradation, playing a key role in proteostasis.
  • Cellular stress necessitates rapid proteome remodeling to support adaptive responses like the DNA damage response (DDR).

Purpose of the Study:

  • To review the role of the ubiquitin system in proteostasis-mediated DDR regulation.
  • To explore the therapeutic potential of targeting ubiquitin system components in cancer treatment.

Main Methods:

  • Literature review of studies on the ubiquitin system, proteostasis, and DDR.
  • Analysis of the mechanisms by which ubiquitin regulates protein abundance and signaling dynamics in DDR.
  • Examination of the link between ubiquitin system dysregulation, genomic instability, and disease.

Main Results:

  • The ubiquitin system is essential for precise control of protein abundance and signaling dynamics in the DDR.
  • Ubiquitin-mediated regulation involves both proteolytic degradation and non-proteolytic scaffolding functions.
  • Dysregulation of the ubiquitin system disrupts DDR control, leading to genomic instability and disease.

Conclusions:

  • Targeting key components of the ubiquitin system can restore proper DDR signaling.
  • Modulating the ubiquitin system presents novel therapeutic opportunities for cancer treatment.
  • Understanding ubiquitin's role in proteostasis and DDR is critical for developing effective cancer therapies.