Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Cells, Cultured, Cytoplasm, Genes, Reporter, Hippocampus, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neuronal Plasticity, Neurons, RNA Splicing, Rats, Receptors, N-Methyl-D-Aspartate, Recombinant Fusion Proteins, Signal Transduction
Amino Acid Sequence, Animals, Base Sequence, Cells, Cultured, Cytoplasm, Genes, Reporter, Hippocampus, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neuronal Plasticity, Neurons, RNA Splicing, Rats, Receptors, N-Methyl-D-Aspartate, Recombinant Fusion Proteins, Signal Transduction
Science
Date: Sep. 22, 1995
PubMed ID: 7569905
View in: Pubmed Google Scholar
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