Identification of calponin as a novel substrate of Rho-kinase.

@article{Kaneko2000IdentificationOC,
  title={Identification of calponin as a novel substrate of Rho-kinase.},
  author={Tetsuo Kaneko and Mutsuki Amano and Atsuyo Maeda and Hiroaki Goto and Koichi Takahashi and Masaaki Ito and Kozo Kaibuchi},
  journal={Biochemical and biophysical research communications},
  year={2000},
  volume={273 1},
  pages={110-6}
}
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 Ca(2+)/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… CONTINUE READING
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