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J. Cell Biol.,
Volume 141, Number 2, April 20, 1998 409-418
* Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-0101, Japan; The small GTPase Rho is believed to regulate the actin cytoskeleton and cell adhesion through its
specific targets. We previously identified the Rho targets: protein kinase N, Rho-associated kinase (Rho-
kinase), and the myosin-binding subunit (MBS) of myosin phosphatase. We found that in MDCK epithelial
cells, MBS accumulated at the tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling area,
where moesin, a member of the ERM (ezrin, radixin, and moesin) family, was localized. Neither membrane
ruffling nor an accumulation of moesin and MBS at the
free-end plasma membrane was induced when MDCK
cells were stimulated with TPA after the microinjection
of C3, which ADP-ribosylates and inactivates Rho. MBS was colocalized with moesin at the cell-cell contact sites in MDCK cells. We also found that moesin
was coimmunoprecipitated with MBS from MDCK
cells. Recombinant MBS interacted with the amino-terminal domains of moesin and ezrin. Myosin phosphatase composed of the catalytic subunit and MBS
showed phosphatase activity toward moesin, which was
phosphorylated by Rho-kinase. The phosphatase activity was inhibited when MBS was phosphorylated by
Rho-kinase. These results suggest that MBS is recruited
with moesin to the plasma membrane and that myosin
phosphatase and Rho-kinase regulate the phosphorylation state of moesin downstream of Rho.
Department of Oncology,
Kumamoto University School of Medicine, Kumamoto 860-0811, Japan; and § Department of Virology II, National Institute of
Infectious Diseases, Tokyo 162-0052, Japan
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