The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle

Cell Death Differ. 2005 Sep;12(9):1191-7. doi: 10.1038/sj.cdd.4401702.

Abstract

Owing to the intensive research activity on protein synthesis, little attention was paid in the 1950s and 1960s to protein degradation. However, work by my group and others between 1970 and 1990 led to the identification of the ubiquitin-dependent degradation system. We found that this system contains three types of enzymes: E1 ubiquitin--activating enzyme, E2 ubiquitin--carrier enzyme and E3 ubiquitin--protein ligase. The sequential action of these enzymes leads to conjugation of ubiquitin to proteins and then in most cases to their degradation. This review briefly tells the story of how this pathway was discovered describing the main findings that during the years allowed us to draw the complex picture we have now.

Publication types

  • Historical Article
  • Review

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Biochemistry / history*
  • Carrier Proteins / chemistry
  • Cell Division
  • History, 20th Century
  • Humans
  • Models, Biological
  • Muramidase / chemistry
  • Proteasome Endopeptidase Complex / chemistry
  • Proteins / metabolism
  • Time Factors
  • Ubiquitin / chemistry*
  • Ubiquitin / metabolism
  • Ubiquitin-Activating Enzymes / metabolism
  • Ubiquitin-Protein Ligase Complexes / metabolism
  • Ubiquitin-Protein Ligases / chemistry

Substances

  • Carrier Proteins
  • Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome
  • Ubiquitin-Protein Ligases
  • Muramidase
  • Proteasome Endopeptidase Complex
  • Ubiquitin-Activating Enzymes