Feedback inactivation of D-serine synthesis by NMDA receptor-elicited translocation of serine racemase to the membrane.

ABSTRACT: D-serine is a physiological coagonist of N-methyl D-aspartate receptors (NMDARs) that plays a major role in several NMDAR-dependent events. In this study we investigate mechanisms regulating D-serine production by the enzyme serine racemase (SR). We now report that NMDAR activation promotes translocation of SR to the plasma membrane, which dramatically reduces the enzyme activity. Membrane-bound SR isolated from rat brain is not extracted from the membrane by high detergent and salt concentration, indicating a strong association. Colocalization studies indicate that most membrane-bound SR is located at the plasma membrane and dendrites, with much less SR observed in other types of membrane. NMDAR activation promotes translocation of the cytosolic SR to the membrane, resulting in reduced D-

SUBMITTER: Balan L 

PROVIDER: S-EPMC2678608 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature