Sci. STKE, 6 June 2000
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).
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