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Updated: Nov 21, 2025

Yeast As a Chassis for Developing Functional Assays to Study Human P53
14:57

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Published on: August 4, 2019

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p53, A Victim of the Prion Fashion

Olivier Billant1, Gaëlle Friocourt2, Pierre Roux1

  • 1CRBM, CNRS, UMR5234, 34293 Montpellier, France.

Cancers
|January 16, 2021
PubMed

Insights

The tumor suppressor gene p53, crucial in cancer, can form amyloid aggregates. This review questions the "prion p53" hypothesis by examining p53

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • p53, initially identified as an oncogene, is now recognized as a critical tumor suppressor gene.
  • It regulates over 3000 target genes and numerous cellular functions.
  • Elevated p53 mutations in human cancers prompt investigation into mutant p53 roles.

Purpose of the Study:

  • To challenge the "prion p53" hypothesis.
  • To review evidence of p53 behavior in the context of amyloid proteins, prionoids, and prions.

Main Methods:

  • Literature review and critical analysis of existing data.
  • Comparison of p53 aggregation properties with known prion and amyloid behaviors.

Main Results:

  • Mutant and isoform p53 proteins exhibit dominant-negative and gain-of-function properties.
  • p53 can form amyloid aggregates, exhibiting prion-like characteristics.
  • The "prion p53" hypothesis is critically examined against current prion science.

Conclusions:

  • The prion-like behavior of p53 warrants further investigation.
  • Understanding p53 aggregation is crucial for cancer research.
  • This review provides a nuanced perspective on p53's role in disease.
Keywords:
PMDaggregationamyloidisoformp53prion

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