
pmid: 20493854
Serine racemase (SR) catalyses the synthesis of the transmitter/neuromodulator d‐serine, which plays a major role in synaptic plasticity and N‐methyl d‐aspartate receptor neurotoxicity. We now report that SR is phosphorylated at Thr71 and Thr227 as revealed by mass spectrometric analysis and in vivo phosphorylation assays. Thr71 phosphorylation was observed in the cytosolic and membrane‐bound SR while Thr227 phosphorylation was restricted to the membrane fraction. The Thr71 site has a motif for proline‐directed kinases and is the main phosphorylation site of SR. Experiments with a phosphorylation‐deficient SR mutant indicate that Thr71 phosphorylation increases SR activity, suggesting a novel mechanism for regulating d‐serine production.
Protein Structure, Secondary, 104002 Analytische Chemie, Gliotransmission, Serine racemase, 106002 Biochemie, Racemases and Epimerases, 301204 Pharmakognosie, Mass Spectrometry, Protein Structure, Secondary, Cell Line, Mice, 106023 Molekularbiologie, 104002 Analytical chemistry, Tandem Mass Spectrometry, Cell Line, Tumor, Serine, Animals, Humans, 301204 Pharmacognosy, Phosphorylation, Chromatography, Liquid, Tumor, 106002 Biochemistry, 106023 Molecular biology, NMDA receptor, d-Serine, Glutamate, Chromatography, Liquid
Protein Structure, Secondary, 104002 Analytische Chemie, Gliotransmission, Serine racemase, 106002 Biochemie, Racemases and Epimerases, 301204 Pharmakognosie, Mass Spectrometry, Protein Structure, Secondary, Cell Line, Mice, 106023 Molekularbiologie, 104002 Analytical chemistry, Tandem Mass Spectrometry, Cell Line, Tumor, Serine, Animals, Humans, 301204 Pharmacognosy, Phosphorylation, Chromatography, Liquid, Tumor, 106002 Biochemistry, 106023 Molecular biology, NMDA receptor, d-Serine, Glutamate, Chromatography, Liquid
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