APC/C and SCF: controlling each other and the cell cycle

Curr Biol. 2004 Sep 21;14(18):R787-96. doi: 10.1016/j.cub.2004.09.020.


Regulated protein degradation has emerged as a key recurring theme in multiple aspects of cell-cycle regulation. Importantly, the irreversible nature of proteolysis makes it an invaluable complement to the intrinsically reversible regulation through phosphorylation and other post-translational modifications. Consequently, ubiquitin-protein ligases, the protagonists of regulated protein destruction, have gained prominence that compares to that of the cyclin-dependent kinases (Cdks) in driving the eukaryotic cell-cycle clock. This review will focus on the two main players, the related ubiquitin-protein ligases APC/C and SCF, and how they control cell-cycle progression. I will also try to delineate the regulation and interplay of these destruction mechanisms, which are intricately connected to the kinase network as well as to extrinsic signals. Moreover, cell-cycle ubiquitin-protein ligases are themselves subject to proteolytic control in cis as well as in trans. Finally, a careful comparison of the functions and regulation of APC/C and SCF shows that, in certain aspects, their logic of action is fundamentally different.

Publication types

  • Review

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Cell Cycle / physiology*
  • Eukaryotic Cells / physiology*
  • Models, Biological*
  • Phosphorylation
  • SKP Cullin F-Box Protein Ligases / physiology*
  • Signal Transduction / physiology
  • Ubiquitin-Protein Ligase Complexes / physiology*
  • Ubiquitins / physiology*


  • Ubiquitins
  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome
  • SKP Cullin F-Box Protein Ligases