Glutamatergic regulation of serine racemase via reversal of PIP2 inhibition.
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ABSTRACT:
SUBMITTER: Mustafa AK
PROVIDER: S-EPMC2635840 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Publications
Glutamatergic regulation of serine racemase via reversal of PIP2 inhibition.
Mustafa Asif K AK van Rossum Damian B DB Patterson Randen L RL Maag David D Ehmsen Jeffrey T JT Gazi Sadia K SK Chakraborty Anutosh A Barrow Roxanne K RK Amzel L Mario LM Snyder Solomon H SH
Proceedings of the National Academy of Sciences of the United States of America 20090204 8
D-serine is a physiologic coagonist with glutamate at NMDA-subtype glutamate receptors. As D-serine is localized in glia, synaptically released glutamate presumably stimulates the glia to form and release D-serine, enabling glutamate/D-serine cotransmission. We show that serine racemase (SR), which generates D-serine from L-serine, is physiologically inhibited by phosphatidylinositol (4,5)-bisphosphate (PIP2) presence in membranes where SR is localized. Activation of metabotropic glutamate recep ...[more]
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