Characterization of a novel plant PP2C-like protein Ser/Thr phosphatase as a calmodulin-binding protein.

@article{Takezawa2003CharacterizationOA,
  title={Characterization of a novel plant PP2C-like protein Ser/Thr phosphatase as a calmodulin-binding protein.},
  author={Daisuke Takezawa},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 39},
  pages={38076-83}
}
Protein phosphatases regulated by calmodulin (CaM) mediate the action of intracellular Ca2+ and modulate functions of various target proteins by dephosphorylation. In plants, however, the role of Ca2+ in the regulation of protein dephosphorylation is not well understood due to a lack of information on characteristics of CaM-regulated protein phosphatases. Screening of a cDNA library of the moss Physcomitrella patens by using 35S-labeled calmodulin as a ligand resulted in identification of a… CONTINUE READING

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