Phosphorylation and activation of myosin by Rho-associated kinase (Rho- kinase)

Mutsuki Amano, Masaaki Ito, Kazushi Kimura, Yuko Fukata, Kazuyasu Chihara, Takeshi Nakano, Yoshiharu Matsuura, Kozo Kaibuchi

研究成果: ジャーナルへの寄稿学術論文査読

1733 被引用数 (Scopus)

抄録

The small GTPase Rho is implicated in physiological functions associated with actin-myosin filaments such as cytokinesis, cell motility, and smooth muscle contraction. We have recently identified and molecularly cloned Rho- associated serine/threonine kinase (Rho-kinase), which is activated by GTP·Rho (Matsui, T., Amano, M., Yamamoto, T., Chihara, K., Nakafuku, M., Ito, M., Nakano, T., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996) EMBO J. 15, 2208-2216). Here we found that Rho-kinase stoichiometrically phosphorylated myosin light chain (MLC). Peptide mapping and phosphoamino acid analyses revealed that the primary phosphorylation site of MLC by Rho- kinase was Ser-19, which is the site phosphorylated by MLC kinase. Rho- kinase phosphorylated recombinant MLC, whereas it failed to phosphorylate recombinant MLC, which contained Ala substituted for both Thr-18 and Ser-19. We also found that the phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase. Thus, it is likely that once Rho is activated, then it can interact with Rho-kinase and activate it. The activated Rho-kinase subsequently phosphorylates MLC. This may partly account for the mechanism by which Rho regulates cytokinesis, cell motility, or smooth muscle contraction.

本文言語英語
ページ(範囲)20246-20249
ページ数4
ジャーナルJournal of Biological Chemistry
271
34
DOI
出版ステータス出版済み - 1996
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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