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USP15 in Cancer and Other Diseases: From Diverse Functionsto Therapeutic Targets

Yan-Chi Li1, Song-Wang Cai2, Yu-Bin Shu1

  • 1Department of Cell Biology & Institute of Biomedicine, MOE Key Laboratory of Tumor Molecular Biology, Guangdong Provincial Key Laboratory of Bioengineering Medicine, National Engineering Research Center of Genetic Medicine, College of Life Science and Technology, Jinan University, Guangzhou 510632, China.

Biomedicines
|February 25, 2022
PubMed

Insights

Protein deubiquitination by ubiquitin-specific protease 15 (USP15) is crucial for cell stability and disease regulation. USP15

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Protein ubiquitination and deubiquitination are vital for protein stability and signal pathway regulation.
  • Perturbations in protein homeostasis are linked to various diseases.
  • Deubiquitinating enzymes (DUBs) remove ubiquitin from proteins, with USP15 being a key DUB involved in cellular processes and tumorigenesis.

Purpose of the Study:

  • To review the diverse biological functions of USP15 in cancers and other diseases.
  • To elucidate the complex and often conflicting roles of USP15 in pathological processes.
  • To highlight USP15 as a potential therapeutic target.

Main Methods:

  • Literature review of studies on USP15.
  • Analysis of USP15's structural uniqueness (dislocation catalytic triplet).
  • Examination of reported USP15 substrate functions and disease associations.

Main Results:

  • USP15 exhibits a unique structural conformation compared to other USP enzymes.
  • USP15's role in cancer is context-dependent, acting as both an oncogene and a tumor suppressor.
  • Conflicting reports on USP15 substrate functions highlight its complexity.

Conclusions:

  • The precise role of USP15 in disease pathogenesis remains incompletely understood.
  • USP15's dual role in cancer necessitates further investigation.
  • USP15 represents a promising therapeutic target for various diseases.
Keywords:
USP15cancerdeubiquitinatasetargetubiquitin

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