Essential roles of E3 ubiquitin ligases in p53 regulation

Sanam Sane, Khosrow Rezvani

Research output: Contribution to journalReview articlepeer-review

53 Scopus citations


The ubiquitination pathway and proteasomal degradation machinery dominantly regulate p53 tumor suppressor protein stability, localization, and functions in both normal and cancerous cells. Selective E3 ubiquitin ligases dominantly regulate protein levels and activities of p53 in a large range of physiological conditions and in response to cellular changes induced by exogenous and endogenous stresses. The regulation of p53’s functions by E3 ubiquitin ligases is a complex process that can lead to positive or negative regulation of p53 protein in a context- and cell type-dependent manner. Accessory proteins bind and modulate E3 ubiquitin ligases, adding yet another layer of regulatory control for p53 and its downstream functions. This review provides a comprehensive understanding of p53 regulation by selective E3 ubiquitin ligases and their potential to be considered as a new class of biomarkers and therapeutic targets in diverse types of cancers.

Original languageEnglish (US)
Article number442
JournalInternational journal of molecular sciences
Issue number2
StatePublished - Feb 17 2017
Externally publishedYes


  • Apoptosis
  • Cancer therapy
  • E3 ubiquitin ligases
  • Tumor
  • p53 tumor suppressor protein

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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