Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues.

@article{Hayashi1999ImmunofluorescenceDO,
  title={Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues.},
  author={K Hayashi and S Yonemura and T Matsui and S Tsukita},
  journal={Journal of cell science},
  year={1999},
  volume={112 ( Pt 8)},
  pages={1149-58}
}
  • K Hayashi, S Yonemura, +1 author S Tsukita
  • Published 1999 in Journal of cell science
Ezrin/radixin/moesin (ERM) proteins are thought to play an important role in organizing cortical actin-based cytoskeletons through cross-linkage of actin filaments with integral membrane proteins. Recent in vitro biochemical studies have revealed that ERM proteins phosphorylated on their COOH-terminal threonine residue (CPERMs) are active in their cross-linking activity, but this has not yet been evaluated in vivo. To immunofluorescently visualize CPERMs in cultured cells as well as tissues… CONTINUE READING
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