Redundant ubiquitin ligase activities regulate wee1 degradation and mitotic entry

Anthony Smith, Scott Simanski, Mohammad Fallahi, Nagi G. Ayad

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


The irreversible nature of mitotic entry is due to the activation of mitosis specific kinases such as cdk1/cyclin B. Cdk1/cyclin B induces activation of mitosis by promoting phosphatases while suppressing inhibitory factors such as the tyrosine kinase wee1. Since wee1 inactivates cdk1/cyclin B during the S and G2 phases, its activity must be downregulated for mitotic progression to occur. One mechanism of suppressing wee1 activity is ubiquitin-dependent proteolysis. Cdk1/cyclin B1 phosphorylates wee1, targeting it for recognition by ubiquitin ligases and subsequent proteasomal degradation. One of the ubiquitin ligases promoting wee1 destruction during mitosis is the SCFβ-trcp complex. We demonstrate that this complex, and a second SCF complex containing the F-box protein Tome-1, regulate wee1 degradation during the S and G2 phases of the cell cycle. Therefore, redundant ubiquitin ligase activities promote efficient mitotic entry of eukaryotic cells.

Original languageEnglish (US)
Pages (from-to)2795-2799
Number of pages5
JournalCell Cycle
Issue number22
StatePublished - Nov 15 2007
Externally publishedYes


  • β-TRCP
  • Degradation
  • F-box
  • Mitosis
  • Tome-1
  • Wee1

ASJC Scopus subject areas

  • Cell Biology
  • Biochemistry
  • Molecular Biology


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