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© The Rockefeller University Press, 0021-9525/1998//409 $5.00
The Journal of Cell Biology, Volume 141, Number 2, , 1998 409-418

Articles

Association of the Myosin-binding Subunit of Myosin Phosphatase and Moesin: Dual Regulation of Moesin Phosphorylation by Rho-associated Kinase and Myosin Phosphatase



Yuko Fukata*, Kazushi Kimura*, Noriko Oshiro*, Hideyuki Saya{ddagger}, Yoshiharu Matsuura§, and Kozo Kaibuchi*

* Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-0101, Japan; {ddagger} 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

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.

Abbreviations used in this paper: aa, amino acids; A-PMSF, (p-amidinophenyl)-methanesulfonyl fluoride; C-moesin, COOH-terminal domain of moesin; ERM, ezrin, radixin, and moesin; GDI, GDP dissociation inhibitor; GST, glutathione-S-transferase; HA, hemagglutinin; MBS, myosin-binding subunit; MLC, myosin light chain; 4,5-PIP2, phosphatidylinositol 4,5-diphosphate; PI5-kinase, phosphatidylinositol 5-kinase; Rho-kinase, Rho-associated kinase; TPA, tetradecanoylphorbol-13-acetate.

This investigation was supported by grants-in-aid for Scientific Research and for Cancer Research from the Ministry of Education, Science, and Culture, Japan (1997) and by grants from the Mitsubishi Foundation and Kirin Brewery Company Limited.

Address all correspondence to Kozo Kaibuchi, M.D. and Ph.D., Division of Signal Transduction, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan, Tel.: 81-743-72-5440. Fax: 81-743-72-5449. E-mail: kaibuchi{at}bs.aist-nara.ac.jp


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