Proteolysis and the G1-S transition: the SCF connection

Curr Opin Genet Dev. 1998 Feb;8(1):36-42. doi: 10.1016/s0959-437x(98)80059-2.


Temporal control of ubiquitin-proteasome mediated protein degradation is critical for normal G1 and S phase progression. Recent work has shown that central to the temporal control mechanism is a relationship between newly identified E3 ubiquitin protein ligases, designated SCFs (Skp1-cullin-F-box protein ligase complexes), which confer substrate specificity on ubiquitination reactions and the activities of protein kinases that phosphorylate substrates destined for destruction at specific sites, thereby converting them into preferred targets for ubiquitin modification catalyzed by SCFs. The constituents of SCFs are members of evolutionary conserved protein families. SCF-based ubiquitination pathways may play a key role in diverse biological processes, such as cell proliferation, differentiation and development.

Publication types

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

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Cell Cycle Proteins / metabolism*
  • Cell Cycle*
  • Cullin Proteins*
  • G1 Phase
  • Humans
  • Ligases / metabolism*
  • Phosphorylation
  • S Phase
  • S-Phase Kinase-Associated Proteins
  • Saccharomyces cerevisiae Proteins*
  • Ubiquitin-Protein Ligase Complexes*
  • Ubiquitin-Protein Ligases
  • Ubiquitins / metabolism


  • Cdc53 protein, S cerevisiae
  • Cell Cycle Proteins
  • Cullin Proteins
  • S-Phase Kinase-Associated Proteins
  • Saccharomyces cerevisiae Proteins
  • Ubiquitins
  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome
  • Ubiquitin-Protein Ligases
  • Ligases