期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 104, 期 8, 页码 2950-2955出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0611620104
关键词
neuronal nitric-oxide synthase; NMDA receptor; S-nitrosylation
资金
- NIDA NIH HHS [K05 DA000074, DA 00074] Funding Source: Medline
- NIMH NIH HHS [MH 18501, R37 MH018501, R01 MH018501] Funding Source: Medline
Serine racemase (SR) generates D-serine, a coagonist with glutamate at NMDA receptors. We show that SR is physiologically S-nitrosylated leading to marked inhibition of enzyme activity. Inhibition involves interactions with the cofactor ATP reflecting juxtaposition of the ATP-binding site and cysteine-113 (C113), the site for physiological S-nitrosylation. NMDA receptor physiologically enhances SR S-nitrosylation by activating neuronal nitric-oxide synthase (nNOS). These findings support a model whereby postsynaptic stimulation of nitric-oxide (NO) formation feeds back to presynaptic cells to S-nitrosylate SR and decrease D-serine availability to postsynaptic NMDA receptors.
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