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Modulation of protein tyrosine phosphatase activity alters the subunit assembly in native N-methyl-D-aspartate

Karima Ferrani-Kile¹, Steven W Leslie

¹Division of Pharmacology and Toxicology, College of Pharmacy and the Waggoner Center for Alcohol and Addiction Research, The University of Texas at Austin, 1 University Station, A1915, Austin, TX 78712, USA. ferrani@mail.utexas.edu

The Journal of Pharmacology and Experimental Therapeutics

|April 20, 2005

Abstract:

The N-methyl-D-aspartate (NMDA) receptor is crucial for development and neuroplasticity as well as excitotoxicity. The biochemical basis of the disassembly and reassembly of NMDA receptor has never been reported. Using coimmunoprecipitation, Western blotting, and mass spectrometry, we show that inhibition of tyrosine phosphatases triggers disassembly of NR1, NR2A, and NR2B in cortical NMDA receptor complexes. Furthermore, the disassembly of the NMDA receptor subunits is immediate, dose-dependent, and reversible and seems to occur through mechanisms linked to Src kinases. Together, these results define a novel role for tyrosine phosphatases in the complex mechanism of NMDA receptor regulation.

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