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Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
H C Kornau1, L T Schenker, M B Kennedy
1Center for Molecular Biology (ZMBH), University of Heidelberg, Germany.
Science (New York, N.Y.)
|September 22, 1995
Summary
The N-methyl-D-aspartate (NMDA) receptor interacts with the postsynaptic density protein PSD-95. This interaction, involving specific protein domains, may influence synaptic plasticity in central neurons.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- The N-methyl-D-aspartate (NMDA) receptor is crucial for synaptic transmission and plasticity in the central nervous system.
- Understanding the molecular mechanisms underlying NMDA receptor function is key to deciphering neuronal communication.
Purpose of the Study:
- To investigate the interaction between NMDA receptor subunits and postsynaptic density protein 95 (PSD-95).
- To identify the specific domains and motifs involved in this protein-protein interaction.
- To explore the potential functional implications of this interaction on synaptic plasticity.
Main Methods:
- Yeast two-hybrid system to screen for interacting proteins.
- Analysis of protein domains, specifically the COOH-terminal and PDZ domains.
- Co-localization studies using cultured rat hippocampal neurons.
Main Results:
- The cytoplasmic tails of NMDA receptor subunits were found to interact with PSD-95.
- The second PDZ domain of PSD-95 specifically binds to a conserved tSXV motif in the COOH-terminus of NR2 subunits and certain NR1 splice forms.
- PSD-95 transcripts show expression patterns similar to NMDA receptors, and NR2B subunits co-localize with PSD-95 in hippocampal neurons.
Conclusions:
- A direct interaction exists between NMDA receptor subunits and PSD-95.
- This interaction is mediated by specific molecular motifs and domains.
- The physical association of NMDA receptors and PSD-95 likely plays a significant role in regulating the plasticity of excitatory synapses.