Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 9 October 2001
Vol. 2001, Issue 103, p. tw373
[DOI: 10.1126/stke.2001.103.tw373]


Cell Cycle Regulating Cell Proliferation

Increased amounts of cyclin E and its protein kinase partner cyclin-dependent kinase 2 (CDK2) promote progression of cells from G1 to S phase of the cell cycle, and the abundance of cyclin E is regulated by proteolysis. Koepp et al. have identified the human ubiquitin ligase subunit, named Fbw7, that binds phosphorylated cyclin E and targets it to the SCF complex, where it is ubiquitinated and later degraded. Thus, similar mechanisms are used in yeast, worms, flies, and mammals to regulate abundance of cyclin E. The functional characterization of Fbw7 suggests that it could function as a tumor suppressor. A Perspective by Bartek and Lukas accompanies the report.

D. M. Koepp, L. K. Scjaefer, X. Ye, K. Keyomarsi, C. Chu, J. W. Harper, S. J. Elledge, Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 294, 173-177 (2001). [Abstract] [Full Text]

J. Bartek, J. Lucas, Orders from destruction, Science 294, 66 (2001). [Full Text]

Citation: Regulating Cell Proliferation. Sci. STKE 2001, tw373 (2001).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882