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J Biol Chem, Vol. 273, Issue 10, 5542-5548, March 6, 1998
§,
,
From the 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. Here we purified MBS-interacting proteins, identified them
as adducin, and found that MBS specifically interacted with adducin in vitro and in vivo. Adducin is a
membrane-skeletal protein that promotes the binding of spectrin to
actin filaments and is concentrated at the cell-cell contact sites in
epithelial cells. We also found that Rho-kinase phosphorylated
Department of Anatomy and Neurobiology,
Graduate School of Medicine, Kyoto University, Konoe-Yoshida, Sakyo-ku,
Kyoto 606, Japan, the § Division of Signal Transduction,
Nara Institute of Science and Technology,
8916-5 Takayama, Ikoma 630-01, Japan, the ¶ Howard Hughes
Medical Institute and Departments of Cell Biology and Biochemistry,
Duke University Medical Center, Durham, North Carolina 27710, the
Department of Virology II, National Institute of Infectious
Diseases, 1-23-1 Toyama, Shinjyuku-ku, Tokyo 162, Japan, and the
** Central Laboratories for Key Technology, Kirin Brewery Company
Limited, 1-13-5 Fukuura, Kanazawa-ku, Yokohama 236, Japan
-adducin in vitro and in vivo and that the
phosphorylation of -adducin by Rho-kinase enhanced the interaction
of -adducin with actin filaments in vitro. Myosin phosphatase composed of the catalytic subunit and MBS showed
phosphatase activity toward -adducin, which was phosphorylated by
Rho-kinase. This phosphatase activity was inhibited by the
phosphorylation of MBS by Rho-kinase. These results suggest that
Rho-kinase and myosin phosphatase regulate the phosphorylation state of
adducin downstream of Rho and that the increased phosphorylation of
adducin by Rho-kinase causes the interaction of adducin with actin
filaments.
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