Protein destruction: adapting roles for Cks proteins

Curr Biol. 2001 Jun 5;11(11):R431-5. doi: 10.1016/s0960-9822(01)00253-6.

Abstract

Cks1, a subunit of cyclin-dependent kinases, has now been identified as an essential cofactor in the ubiquitination of the Cdk inhibitor p27 by the SCF(Skp2) ubiquitin ligase. This activity, which can be independent of Cdk binding, links Cks to positive growth control pathways regulating the G1/S transition and to cancer.

Publication types

  • Review

MeSH terms

  • Cell Cycle Proteins / metabolism*
  • Cyclin-Dependent Kinase Inhibitor p27
  • Cyclin-Dependent Kinases / metabolism*
  • G1 Phase / physiology*
  • Ligases / metabolism*
  • Models, Biological
  • Models, Molecular
  • Protein Binding
  • Protein Processing, Post-Translational
  • Tumor Suppressor Proteins / metabolism*
  • Ubiquitin / metabolism*
  • Ubiquitin-Protein Ligases

Substances

  • Cell Cycle Proteins
  • Tumor Suppressor Proteins
  • Ubiquitin
  • Cyclin-Dependent Kinase Inhibitor p27
  • Ubiquitin-Protein Ligases
  • Cyclin-Dependent Kinases
  • p9(Cks1) protein, human
  • Ligases