Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor.

Proteomic analyses have revealed a novel synaptic proline-rich membrane protein: PRR7 (proline rich 7), in the postsynaptic density (PSD) fraction of rat forebrain. PRR7 is 269 amino acid residues long, and displays a unique architecture, composed of a very short N-terminal extracellular region, a single membrane spanning domain, and a ...
cytoplasmic domain possessing a proline-rich sequence and a C-terminal type-1 PDZ binding motif. A fraction of PRR7 accumulates in spines along with synapse maturation, and colocalizes with PSD-95 in a punctate pattern in rat hippocampal neural cultures. Immunoprecipitation and GST pull-down assays demonstrated that PRR7 binds to the third PDZ domain of PSD-95. In addition, the NMDA receptor subunits, NR1 and NR2B, specifically co-immunoprecipitated with PRR7. These results suggest that PRR7 is involved in modulating neural activities via interactions with the NMDA receptor and PSD-95, and PSD core formation.
Mesh Terms:
Amino Acid Sequence, Animals, Antibodies, Antibody Affinity, Brain, Cells, Cultured, Detergents, Disks Large Homolog 4 Protein, Gene Expression Profiling, Hippocampus, Humans, Immunoprecipitation, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Structure, Tertiary, Protein Transport, Proteomics, Rats, Rats, Wistar, Receptors, N-Methyl-D-Aspartate, Sequence Alignment, Solubility, Tissue Extracts
Biochem. Biophys. Res. Commun.
Date: Feb. 04, 2005
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