Regulation of the association of adducin with actin filaments by Rho- associated kinase (Rho-kinase) and myosin phosphatase

Kazushi Kimura, Yuko Fukata, Yoichiro Matsuoka, Vann Bennett, Yoshiharu Matsuura, Katsuya Okawa, Akihiro Iwamatsu, Kozo Kaibuchi

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182 Citations (Scopus)


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 α-adducin in vitro and in vivo and that the phosphorylation of α-adducin by Rho-kinase enhanced the interaction of α-adducin with actin filaments in vitro. Myosin phosphatase composed of the catalytic subunit and MBS showed phosphatase activity toward α-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.

Original languageEnglish
Pages (from-to)5542-5548
Number of pages7
JournalJournal of Biological Chemistry
Issue number10
Publication statusPublished - 06-03-1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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