RT Journal Article
SR Electronic
T1 New Role for Zyxin
JF Science's STKE
JO Sci. STKE
FD American Association for the Advancement of Science
SP tw8
OP tw8
DO 10.1126/stke.2000.35.tw8
VO 2000
IS 35
YR 2000
UL http://stke.sciencemag.org/content/2000/35/tw8.abstract
AB 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]