No PUMA, no death: implications for p53-dependent apoptosis

Cancer Cell. 2003 Oct;4(4):248-9. doi: 10.1016/s1535-6108(03)00249-6.

Abstract

More than a decade ago, it was found that one of the two essential physiological functions of p53 is to selectively destroy stressed cells through apoptosis. Despite the large number of studies describing p53-dependent apoptosis since then, how p53 turns on the apoptotic switch has remained enigmatic. In this issue of Cancer Cell, Jeffers et al. report that knockout of PUMA, a recently identified BH3-only Bcl-2 family protein, recapitulates virtually all apoptotic deficiency in p53 knockout mice. Their results indicate that PUMA is an essential mediator of p53-dependent and -independent apoptosis in vivo.

Publication types

  • Review

MeSH terms

  • Animals
  • Apoptosis / physiology*
  • Apoptosis Regulatory Proteins
  • Cell Hypoxia / physiology
  • DNA Damage / drug effects
  • DNA Damage / physiology
  • Mice
  • Mice, Knockout
  • Mutation
  • Oxidative Stress / physiology
  • Protein-Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Signal Transduction
  • Tumor Suppressor Protein p53 / metabolism*
  • bcl-2-Associated X Protein
  • p21-Activated Kinases

Substances

  • Apoptosis Regulatory Proteins
  • BBC3 protein, human
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Tumor Suppressor Protein p53
  • bcl-2-Associated X Protein
  • Protein-Serine-Threonine Kinases
  • p21-Activated Kinases