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Originally published in Science Express on 30 August 2001
Science 5 October 2001:
Vol. 294. no. 5540, pp. 173 - 177
DOI: 10.1126/science.1065203
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Reports

Phosphorylation-Dependent Ubiquitination of Cyclin E by the SCFFbw7 Ubiquitin Ligase

Deanna M. Koepp,123 Laura K. Schaefer,123* Xin Ye,1* Khandan Keyomarsi,4 Claire Chu,1 J. Wade Harper,1 Stephen J. Elledge123dagger

Cyclin E binds and activates the cyclin-dependent kinase Cdk2 and catalyzes the transition from the G1 phase to the S phase of the cell cycle. The amount of cyclin E protein present in the cell is tightly controlled by ubiquitin-mediated proteolysis. Here we identify the ubiquitin ligase responsible for cyclin E ubiquitination as SCFFbw7 and demonstrate that it is functionally conserved in yeast, flies, and mammals. Fbw7 associates specifically with phosphorylated cyclin E, and SCFFbw7 catalyzes cyclin E ubiquitination in vitro. Depletion of Fbw7 leads to accumulation and stabilization of cyclin E in vivo in human and Drosophila melanogaster cells. Multiple F-box proteins contribute to cyclin E stability in yeast, suggesting an overlap in SCF E3 ligase specificity that allows combinatorial control of cyclin E degradation.

1 Department of Biochemistry and Molecular Biology,
2 Department of Molecular and Human Genetics,
3 Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX, 77030, USA.
4 Department of Experimental Radiation Oncology, M. D. Anderson Cancer Center, Houston, TX 77030, USA
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: selledge{at}bcm.tmc.edu

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