Substrate recognition and ubiquitination of SCFSkp2/Cks1 ubiquitin-protein isopeptide ligase

J Biol Chem. 2007 May 25;282(21):15462-70. doi: 10.1074/jbc.M610758200. Epub 2007 Apr 4.

Abstract

p27, an important cell cycle regulator, blocks the G(1)/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr(187) on p27 are essential for the recognition of p27 by the SCF(Skp2/Cks1) complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr(187) provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CDC2-CDC28 Kinases
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Cell-Free System / chemistry
  • Cell-Free System / metabolism
  • Cyclin A / chemistry
  • Cyclin A / metabolism
  • Cyclin E / chemistry
  • Cyclin E / metabolism
  • Cyclin-Dependent Kinase 2 / chemistry
  • Cyclin-Dependent Kinase 2 / metabolism
  • Cyclin-Dependent Kinase Inhibitor p27 / chemistry
  • Cyclin-Dependent Kinase Inhibitor p27 / metabolism
  • Cyclin-Dependent Kinases / chemistry*
  • Cyclin-Dependent Kinases / metabolism
  • G1 Phase / physiology
  • Humans
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / metabolism
  • Phosphorylation
  • Protein Processing, Post-Translational* / physiology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • S Phase / physiology
  • S-Phase Kinase-Associated Proteins / chemistry*
  • S-Phase Kinase-Associated Proteins / metabolism
  • Ubiquitin-Protein Ligases / chemistry*
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • CKS1B protein, human
  • Carrier Proteins
  • Cyclin A
  • Cyclin E
  • Multiprotein Complexes
  • Recombinant Proteins
  • S-Phase Kinase-Associated Proteins
  • Cyclin-Dependent Kinase Inhibitor p27
  • Ubiquitin-Protein Ligases
  • CDC2-CDC28 Kinases
  • CDK2 protein, human
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases