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, 27 July 2004
Vol. 2004, Issue 243, p. tw274
[DOI: 10.1126/stke.2432004tw274]


CELL CYCLE Getting Out of Mitosis

The protein phosphatase Cdc14 controls a number of the late events of mitosis. Cdc14 is sequestered in the nucleolus, but late in mitosis, it is released and moves throughout the cell to help to coordinate the exit from mitosis. Cdc14 is held in the nucleus through interaction with a protein called Net1. Azzam et al. show that release of Cdc14 appears to depend on phosphorylation of Net1 by the master regulator of mitosis, the complex of cyclin B and cyclin-dependent kinase.

R. Azzam, S. L. Chen, W. Shou, A. S. Mah, G. Alexandru, K. Nasmyth, R. S. Annan, S. A. Carr, R. J. Deshaies, Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus. Science 305, 516-519 (2004). [Abstract] [Full Text]

Citation: Getting Out of Mitosis. Sci. STKE 2004, tw274 (2004).

To Advertise     Find Products

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