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PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain

Christopherson, K S ; Hillier, B J ; Lim, W A ; Bredt, D S

The Journal of biological chemistry, 1999-09, Vol.274 (39), p.27467-27473 [Periódico revisado por pares]

United States

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Título:
PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain
Autor: Christopherson, K S ; Hillier, B J ; Lim, W A ; Bredt, D S
Assuntos: Animals ; Binding Sites ; Cell Line ; Cell Membrane - physiology ; Cell Membrane - ultrastructure ; Circular Dichroism ; Cloning, Molecular ; Disks Large Homolog 4 Protein ; Guanidine - pharmacology ; Humans ; Intracellular Signaling Peptides and Proteins ; Macromolecular Substances ; Membrane Proteins ; Models, Molecular ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Nitric Oxide Synthase - chemistry ; Nitric Oxide Synthase - metabolism ; Nitric Oxide Synthase Type I ; postsynaptic density 95 protein ; Prosencephalon - metabolism ; Protein Conformation ; Rats ; receptor clustering ; Receptors, N-Methyl-D-Aspartate - chemistry ; Receptors, N-Methyl-D-Aspartate - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Transfection
É parte de: The Journal of biological chemistry, 1999-09, Vol.274 (39), p.27467-27473
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Descrição: Nitric oxide (NO) biosynthesis in cerebellum is preferentially activated by calcium influx through N-methyl-D-aspartate (NMDA)-type glutamate receptors, suggesting that there is a specific link between these receptors and neuronal NO synthase (nNOS). Here, we find that PSD-95 assembles a postsynaptic protein complex containing nNOS and NMDA receptors. Formation of this complex is mediated by the PDZ domains of PSD-95, which bind to the COOH termini of specific NMDA receptor subunits. In contrast, nNOS is recruited to this complex by a novel PDZ-PDZ interaction in which PSD-95 recognizes an internal motif adjacent to the consensus nNOS PDZ domain. This internal motif is a structured "pseudo-peptide" extension of the nNOS PDZ that interacts with the peptide-binding pocket of PSD-95 PDZ2. This asymmetric interaction leaves the peptide-binding pocket of the nNOS PDZ domain available to interact with additional COOH-terminal PDZ ligands. Accordingly, we find that the nNOS PDZ domain can bind PSD-95 PDZ2 and a COOH-terminal peptide simultaneously. This bivalent nature of the nNOS PDZ domain further expands the scope for assembly of protein networks by PDZ domains.
Editor: United States
Idioma: Inglês

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PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain

Christopherson, K S ; Hillier, B J ; Lim, W A ; Bredt, D S

United States

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