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Modulation of the p53/MDM2 interplay by HAUSP inhibitors

Omid Tavana1,2, Wei Gu1,2,3

  • 1College of Physicians and Surgeons, Institute for Cancer Genetics, Columbia University, New York, NY 10032, USA.

Journal of Molecular Cell Biology
|December 9, 2016
PubMed

Insights

The herpesvirus-associated ubiquitin-specific protease (HAUSP) regulates p53 stability. Inhibiting HAUSP increases p53 levels, offering potential cancer therapies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • p53 and MDM2 are short-lived proteins regulated by ubiquitination-mediated degradation.
  • MDM2 E3 ligase activity and p53-MDM2 interaction are key regulatory mechanisms.
  • Emerging evidence highlights the critical role of deubiquitinase HAUSP (USP7) in this pathway.

Purpose of the Study:

  • To review advances in the p53-MDM2-HAUSP regulatory pathway.
  • To discuss positive and negative regulators of HAUSP activity.
  • To highlight HAUSP's role in cancer and the development of inhibitors.

Main Methods:

  • Literature review of studies on p53, MDM2, and HAUSP (USP7).
  • Analysis of regulatory mechanisms controlling HAUSP activity.
  • Examination of HAUSP's role in oncogenesis and therapeutic targeting.

Main Results:

  • HAUSP (USP7) deubiquitinase activity is critical for p53 regulation.
  • HAUSP inhibition enhances p53 protein stability.
  • This pathway's dysregulation is implicated in cancer development.

Conclusions:

  • HAUSP is a key regulator of p53 stability, distinct from MDM2's E3 ligase function.
  • Targeting HAUSP offers a promising therapeutic strategy for cancer.
  • The development of HAUSP inhibitors is a significant advancement in cancer therapy.
Keywords:
HAUSPHAUSP inhibitorsMDM2 stabilityUSP7cancerp53 stability

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