Abstract
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 Cln2p, 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 263-274 |
| Number of pages | 12 |
| Journal | Cell |
| Volume | 86 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 26 1996 |
| Externally published | Yes |
Funding
Correspondence should be addressed to S. J. E. We thank M. Tyers, M. Mendenhall, A. George, L. Johnston, B. Futcher, F. Cross, S. Johnson, H. Zhang, and M. Kuroda for comments, helpful discussions, and/or reagents. We thank C. Connelly, P. Hieter, J. Rosamond, and M. Tyers for sharing results prior to publication. We thank D. Leibham for excellent technical support. This work was supported by a NIH grants GM44664 and AG11085. S. J. E. is a PEW Scholar in the Biomedical Sciences and an Investigator of the Howard Hughes Medical Institute.
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology