Inhibition of zipper-interacting protein kinase function in smooth muscle by a myosin light chain kinase pseudosubstrate peptide.

@article{Ihara2007InhibitionOZ,
  title={Inhibition of zipper-interacting protein kinase function in smooth muscle by a myosin light chain kinase pseudosubstrate peptide.},
  author={Eikichi Ihara and Elena Edwards and Meredith A. Borman and David P Wilson and M. P. Walsh and Justin A. MacDonald},
  journal={American journal of physiology. Cell physiology},
  year={2007},
  volume={292 5},
  pages={C1951-9}
}
As a regulator of smooth muscle contractility, zipper-interacting protein kinase (ZIPK) appears to phosphorylate the regulatory myosin light chain (RLC20), directly or indirectly, at Ser19 and Thr18 in a Ca(2+)-independent manner. The calmodulin-binding and autoinhibitory domain of myosin light chain kinase (MLCK) shares similarity to a sequence found in ZIPK. This similarity in sequence prompted an investigation of the SM1 peptide, which is derived from the autoinhibitory region of MLCK, as a… CONTINUE READING

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