Identification of calponin as a novel substrate of Rho-kinase

Takako Kaneko, Mutsuki Amano, Akio Maeda, Hideyuki Goto, Katsuhito Takahashi, Masaaki Ito, Kozo Kaibuchi

研究成果: ジャーナルへの寄稿学術論文査読

108 被引用数 (Scopus)

抄録

Calponin, an F-actin-associated protein implicated in the regulation of smooth muscle contraction, is known to be phosphorylated in vitro by protein kinase C (PKC) and Ca2+/calmodulin dependent protein kinase II (CaM kinase II). Unphosphorylated calponin binds to F-actin and inhibits the actin-activated myosin ATPase activity; these properties are lost on phosphorylation. In the present study, we found that Rho-kinase phosphorylated basic calponin stoichiometrically in vitro. We identified the sites of phosphorylation of calponin by Rho-kinase as Thr-170, Ser-175, Thr-180, Thr-184, and Thr-259, and prepared antibodies that specifically recognized calponin phosphorylated at Thr-170 and Thr-184. We showed that the phosphorylation of calponin by Rho-kinase inhibited the binding of calponin to F-actin. Taken together, these results suggest that calponin is a substrate of Rho-kinase and that Rho-kinase regulates the interaction of calponin with F-actin. (C) 2000 Academic Press.

本文言語英語
ページ(範囲)110-116
ページ数7
ジャーナルBiochemical and Biophysical Research Communications
273
1
DOI
出版ステータス出版済み - 24-06-2000
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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