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Phosphorylation of mouse serine racemase regulates d ‐serine synthesis
Author(s) -
Foltyn Veronika N.,
Zehl Martin,
Dikopoltsev Elena,
Jensen Ole N.,
Wolosker Herman
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.05.022
Subject(s) - phosphorylation , serine , kinase , cytosol , biochemistry , chemistry , phosphorylation cascade , microbiology and biotechnology , protein phosphorylation , biology , protein kinase a , enzyme
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.