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, 6 June 2000
Vol. 2000, Issue 35, p. tw8
[DOI: 10.1126/stke.2000.35.tw8]


Cell Cycle New Role for Zyxin

Although the serine-threonine kinase h-warts/LATS1 has been implicated in regulating mitosis, its cellular targets have remained elusive. Hirota et al. have now found that it binds to zyxin, a regulator of actin assembly. Interaction required two of the three LIM protein interaction domains of zyxin. During mitosis, a fraction of zyxin, which normally resides at focal adhesion plaques of adherent cells during interphase, localized to the mitotic spindle and poles. Its colocalization at the mitotic apparatus with h-warts/LATS1 required that zyxin be phosphorylated, possibly by the cdc2 kinase. Disruption of the interaction between h-warts/LATS1 and zyxin delayed normal mitotic progression. Hence, zyxin may also regulate actin dynamics during cell division.

Hirota, T., Morisaki, T., Nishiyama, Y., Matumoto, T., Tada, K., Hara, T., Masuko, N., Inagaki, M., Hatakeyama, K., and Saya, H. (2000) Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor. J. Cell Biol. 149: 1073-1086. [Abstract] [Full Text]

Citation: New Role for Zyxin. Sci. STKE 2000, tw8 (2000).

To Advertise     Find Products

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