Regulation of apoptosis by ubiquitination

Immunol Rev. 2003 Jun;193:39-47. doi: 10.1034/j.1600-065x.2003.00043.x.

Abstract

Cell elimination through apoptosis, or programmed cell death, is an evolutionarily conserved central tenet of biology from embryological development to immune homeostasis. While many of the apoptotic signaling pathways have been elucidated, the relationship between ubiquitin and apoptosis is only beginning to be defined. In the past decade, many reports of polyubiquitin conjugation of key pro- and anti-apoptotic molecules have characterized ubiquitin as an essential regulatory modification targeting proteins for proteasomal degradation. However, recent work relating monoubiquitination and nonclassical polyubiquitin conjugation to apoptotic molecules has added an additional level of diversity to the role of ubiquitin in apoptotic regulation beyond degradation. This review focuses on the direct effects of ubiquitination on apoptosis-signaling molecules.

Publication types

  • Review

MeSH terms

  • Animals
  • Apoptosis / physiology*
  • Humans
  • Protein Processing, Post-Translational / physiology*
  • Proteins / metabolism
  • Signal Transduction / physiology*
  • Ubiquitins / metabolism*

Substances

  • Proteins
  • Ubiquitins