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Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains.

Neuronal nitric oxide synthase (nNOS) is concentrated at synaptic junctions in brain and motor endplates in skeletal muscle. Here, we show that the N-terminus of nNOS, which contains a PDZ protein motif, interacts with similar motifs in postsynaptic density-95 protein (PSD-95) and a related novel protein, PSD-93.nNOS and PSD-95 are coexpressed in numerous neuronal populations, and a PSD-95/nNOS complex occurs in cerebellum. PDZ domain interactions also mediate binding of nNOS to skeletal muscle syntrophin, a dystrophin-associated protein. nNOS isoforms lacking a PDZ domain, identified in nNOSdelta/delta mutant mice, do not associate with PSD-95 in brain or with skeletal muscle sarcolemma. Interaction of PDZ-containing domains therefore mediates synaptic association of nNOS and may play a more general role in formation of macromolecular signaling complexes.

Pubmed ID: 8625413


  • Brenman JE
  • Chao DS
  • Gee SH
  • McGee AW
  • Craven SE
  • Santillano DR
  • Wu Z
  • Huang F
  • Xia H
  • Peters MF
  • Froehner SC
  • Bredt DS



Publication Data

March 8, 1996

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Brain
  • Calcium-Binding Proteins
  • Cell Membrane
  • DNA Primers
  • Embryo, Mammalian
  • Exons
  • Gene Expression
  • Guanylate Kinase
  • In Situ Hybridization
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Models, Structural
  • Molecular Sequence Data
  • Muscle Proteins
  • Muscle, Skeletal
  • Nerve Tissue Proteins
  • Neurons
  • Nitric Oxide Synthase
  • Organ Specificity
  • Polymerase Chain Reaction
  • Protein Conformation
  • RNA, Messenger
  • Rats
  • Recombinant Fusion Proteins
  • Signal Transduction
  • Tumor Suppressor Proteins