Targeting ubiquitin specific protease 7 in cancer: A deubiquitinase with great prospects

Farjana Yeasmin Khusbu1, Fang-Zhi Chen2, Han-Chun Chen1

  • 1Department of Biochemistry and Molecular Biology, School of Life Sciences, Central South University, Changsha, Hunan, China.

Insights

Deubiquitinase USP7 regulates protein fate by cleaving ubiquitin chains. Its diverse roles in cellular processes suggest its abnormal activity may promote cancer, highlighting the need for specific inhibitors.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Deubiquitinase (DUB) activity balances ubiquitination, controlling protein fate.
  • USP7 is a well-characterized DUB with significant functional importance.
  • USP7 interacts with numerous proteins involved in critical cellular processes.

Purpose of the Study:

  • To review the extensive roles of USP7 in cellular and biological processes.
  • To explore the link between USP7 dysregulation and oncogenesis.
  • To emphasize the importance of developing USP7-specific inhibitors.

Main Methods:

  • Literature review of studies on USP7.
  • Analysis of USP7 substrates and binding partners.
  • Synthesis of information on USP7's involvement in various cellular functions.

Main Results:

  • USP7 is implicated in tumor suppression, cell cycle regulation, DNA repair, chromatin remodeling, and epigenetic regulation.
  • A wide array of cellular processes are influenced by USP7 activity.
  • Abnormal USP7 function is potentially linked to cancer development.

Conclusions:

  • USP7 plays a critical role in numerous cellular pathways.
  • Understanding USP7's broad associations provides insights into its potential role in cancer.
  • Targeting USP7 with specific inhibitors is a promising therapeutic strategy.

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