Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
Abstract
The N-methyl-D-aspartate (NMDA) receptor subserves synaptic glutamate-induced transmission and plasticity in central neurons. The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95. The second PDZ domain in PSD-95 binds to the seven-amino acid, COOH-terminal domain containing the terminal tSXV motif (where S is serine, X is any amino acid, and V is valine) common to NR2 subunits and certain NR1 splice forms. Transcripts encoding PSD-95 are expressed in a pattern similar to that of NMDA receptors, and the NR2B subunit co-localizes with PSD-95 in cultured rat hippocampal neurons. The interaction of these proteins may affect the plasticity of excitatory synapses.
Additional Information
© 1995 American Association for the Advancement of Science. Received 8 June 1995; accepted 7 August 1995. We thank S. Grunewald, A. Herold, U. Keller, and M. Kiely for technical assistance, L. Van Aelst and J. Zwicker for helpful suggestions, and R. Sprengel for critical reading. H.-C.K. is the recipient of a doctoral fellowship by the Boehringer Ingelheim Funds. Supported by U.S. Public Health Service grant NS-28710 to M.B.K. and SFB (Sonderforschungsbereich) grant 319 and funds of the German Chemical Society to P.H.S.Additional details
- Eprint ID
- 30316
- DOI
- 10.1126/science.7569905
- Resolver ID
- CaltechAUTHORS:20120424-151520271
- Boehringer Ingelheim
- U.S. Public Health Service (USPHS)
- NS-28710
- Sonderforschungsbereich
- SFB 319
- German Chemical Society
- Created
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2012-04-25Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field