FEBS Letters · 1987 · 293 citations · 11 references
Life SciencesBiochemistryNeuroscienceEnzymologyNeurochemistrySignal TransductionAmino Acid NeurochemistryEnzyme FunctionNeurotransmissionNeurotransmitter BiosynthesisNeurotransmitter SystemsSerotonergic SignalingActivator ProteinsCalcium-calmodulin SignalingCalcium-dependent Protein Kinase IiCalmodulin-dependent Protein Kinase IiCalmodulin-mediated RegulationSerotonin BiosynthesisSerotonin SynthesisTryptophan Metabolism
We have found that the 14-3-3 protein, an acidic neuronal protein, is substantially identical to the 'activator' protein [(1981) J. Biol. Chem. 256, 5404-5409] that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+, calmodulin dependent protein kinase II. This finding is based on the remarkable similarity of both these proteins in physicochemical, biochemical and immunochemical properties, as well as on detection for the 14-3-3 protein of an activator activity towards tryptophan 5-monooxygenase. The result suggests that the 14-3-3 protein plays a role in the regulation of serotonin and noradrenaline biosynthesis in brain.
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Takashi Yamauchi, Hitoshi Fujisawa · European Journal of Biochemistry · 1983 · 245 citations · Full text
Takashi Yamauchi, H Nakata, H. Fujisawa · Journal of Biological Chemistry · 1981 · 234 citations · Full text