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Targeting the deubiquitinase USP28 in cancer: navigating context-dependent mechanisms and therapeutic resistance

Tongyong Luo1, Shuncai Wu2, Qingsong Wang3

  • 1Pediatric Cardiology Center, Sichuan Provincial Women's and Children's Hospital/The Affiliated Women's and Children's Hospital of Chengdu Medical College, Chengdu, China.

Frontiers in Immunology
|August 7, 2026
PubMed

Insights

Ubiquitin-specific protease 28 (USP28) is a key enzyme in DNA damage response. Its role in cancer varies, offering potential for targeted therapies and biomarker discovery.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Ubiquitin-specific protease 28 (USP28) is a deubiquitinating enzyme.
  • USP28 regulates proteins like p53 and c-MYC, impacting DNA damage response and cell cycle.
  • It plays a role in maintaining genomic integrity.

Purpose of the Study:

  • To review the molecular characteristics and physiological functions of USP28.
  • To explore USP28's context-dependent roles in neoplastic diseases.
  • To discuss USP28's translational implications for targeted therapy and biomarker discovery.

Main Methods:

  • Literature review of USP28's functions.
  • Analysis of USP28's role in various solid tumors.
  • Examination of USP28's dual role in different cancer types.

Main Results:

  • USP28 is upregulated in lung, pancreatic, ovarian, and hepatocellular carcinomas, promoting cancer progression.
  • It stabilizes oncoproteins like c-Myc, STAT3, and SOX9, driving proliferation and therapeutic resistance.
  • USP28 deficiency can paradoxically drive malignant progression in breast cancer and melanomas.

Conclusions:

  • USP28 exhibits complex, context-dependent signaling in cancer.
  • USP28 is a potential therapeutic target for precision medicine.
  • Further research into USP28 could lead to novel biomarker discovery.
Keywords:
USP28context-dependencydeubiquitinating enzymetherapeutic targettumorigenesis

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