Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins.

@article{Itagaki1999StimuluscoupledIO,
  title={Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins.},
  author={Chiharu Itagaki and Toshiaki Isobe and Masato Taoka and Tohru Natsume and Nobuo Nomura and Tsuneyoshi Horigome and Saburo Omata and Hiroshi Ichinose and Toshiharu Toshi Nagatsu and Lloyd A Greene and Tohru Ichimura},
  journal={Biochemistry},
  year={1999},
  volume={38 47},
  pages={15673-80}
}
Tyrosine hydroxylase (TH) is phosphorylated by CaM kinase II and is activated in situ in response to a variety of stimuli that increase intracellular Ca(2+). We report here, using baculovirus-expressed TH, that the 14-3-3 protein binds and activates the expressed TH when the enzyme is phosphorylated at Ser-19, a site of CaM kinase II-dependent phosphorylation located in the regulatory domain of TH. Site-directed mutagenesis showed that a TH mutant in which Ser-19 was substituted by Ala retained… CONTINUE READING

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