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Publication : Phosphorylation of mouse serine racemase regulates D-serine synthesis.

First Author  Foltyn VN Year  2010
Journal  FEBS Lett Volume  584
Issue  13 Pages  2937-41
PubMed ID  20493854 Mgi Jnum  J:161309
Mgi Id  MGI:4457976 Doi  10.1016/j.febslet.2010.05.022
Citation  Foltyn VN, et al. (2010) Phosphorylation of mouse serine racemase regulates D-serine synthesis. FEBS Lett 584(13):2937-41
abstractText  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.
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