Proteolysis and the cell cycle: with this RING I do thee destroy

Curr Opin Genet Dev. 2000 Feb;10(1):54-64. doi: 10.1016/s0959-437x(99)00049-0.


The ubiquitin system drives the cell division cycle by the timely destruction of numerous regulatory proteins. Remarkably, the two main activities that catalyze substrate ubiquitination in the cell cycle, the Skp1-Cdc53/cullin-F-box protein (SCF) complexes and the anaphase-promoting complex/cyclosome (APC/C), define a new superfamily of E3 ubiquitin ligases, all based on related cullin and RING-H2 finger protein subunits. The circuits that interconnect the SCF, APC/C and cyclin-dependent kinase activities form a master oscillator that coordinates the replication and segregation of the genome.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Cell Cycle / physiology
  • Cyclin-Dependent Kinases / physiology
  • Genes, cdc*
  • Humans
  • Ligases / metabolism*
  • Mitosis / genetics*
  • Mitosis / physiology
  • Peptide Synthases / metabolism*
  • SKP Cullin F-Box Protein Ligases
  • Ubiquitin-Protein Ligase Complexes*
  • Ubiquitin-Protein Ligases
  • Yeasts
  • Zinc Fingers


  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome
  • SKP Cullin F-Box Protein Ligases
  • Ubiquitin-Protein Ligases
  • Cyclin-Dependent Kinases
  • Ligases
  • Peptide Synthases