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Evidence for the ISG15-Specific Deubiquitinase USP18 as an Antineoplastic Target

Lisa Maria Mustachio1, Yun Lu2, Masanori Kawakami1

  • 1Department of Thoracic/Head and Neck Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas.

Cancer Research
|January 19, 2018
PubMed

Insights

Targeting deubiquitinases (DUBs) offers new cancer treatments. Inhibiting USP18, a key DUB, destabilizes cancer-promoting proteins, leading to apoptosis and repressed tumor growth.

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Posttranslational modifications (PTMs) like ubiquitination regulate key cancer proteins.
  • Deubiquitinases (DUBs) are critical enzymes in PTM regulation and are potential antineoplastic targets.
  • Few DUB inhibitors currently exist, highlighting a gap in cancer therapeutics.

Purpose of the Study:

  • To evaluate ubiquitin-specific protease 18 (USP18) as a novel pharmacologic target in oncology.
  • To summarize evidence supporting USP18's role in cancer progression and its potential as a therapeutic target.

Main Methods:

  • Review of existing literature on USP18 function in cancer.
  • Analysis of USP18's role in regulating ISG15 conjugation and its impact on protein stability.
  • Examination of genetic models and tissue expression data to assess USP18's translational relevance.

Main Results:

  • Engineered loss of USP18 increases ISGylation and decreases cancer growth by destabilizing growth-regulatory proteins.
  • USP18 loss triggers apoptosis and represses cancer formation in murine lung cancer models.
  • USP18 expression is deregulated in malignant versus normal tissues, confirming its translational relevance.

Conclusions:

  • USP18 is a significant DUB involved in cancer progression.
  • USP18 inhibition represents a promising therapeutic strategy for cancer treatment.
  • The elucidated USP18 crystal structure provides a basis for developing targeted inhibitors.

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