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SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.

We have identified the yeast and human homologs of the SKP1 gene as a suppressor of cdc4 mutants and as a cyclin F-binding protein. Skp1p indirectly binds cyclin A/Cdk2 through Skp2p, and directly binds Skp2p, cyclin F, and Cdc4p through a novel structural motif called the F-box. SKP1 is required for ubiquitin-mediated proteolysis of Cin2p, Clb5p, and the Cdk inhibitor Sic1p, and provides a link between these molecules and the proteolysis machinery. A large number of proteins contain the F-box motif and are thereby implicated in the ubiquitin pathway. Different skp1 mutants arrest cells in either G1 or G2, suggesting a connection between regulation of proteolysis in different stages of the cycle.

Pubmed ID: 8706131


  • Bai C
  • Sen P
  • Hofmann K
  • Ma L
  • Goebl M
  • Harper JW
  • Elledge SJ



Publication Data

July 26, 1996

Associated Grants

  • Agency: NIA NIH HHS, Id: AG11085
  • Agency: NIGMS NIH HHS, Id: GM44664

Mesh Terms

  • Amino Acid Sequence
  • Anaphase-Promoting Complex-Cyclosome
  • Base Sequence
  • Binding Sites
  • Cell Cycle
  • Cell Cycle Proteins
  • Cyclins
  • F-Box Proteins
  • Fungal Proteins
  • G1 Phase
  • G2 Phase
  • Gene Dosage
  • Gene Expression
  • Humans
  • Ligases
  • Mitosis
  • Molecular Sequence Data
  • Molecular Structure
  • Mutation
  • Protein Structure, Tertiary
  • Proteins
  • S Phase
  • S-Phase Kinase-Associated Proteins
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin-Protein Ligase Complexes
  • Ubiquitin-Protein Ligases
  • Ubiquitins
  • Yeasts