Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON Academic Article uri icon

Overview

MeSH Major

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Neurons
  • Nitric Oxide Synthase
  • Synapsins

abstract

  • The specificity of the reactions of nitric oxide (NO) with its neuronal targets is determined in part by the precise localizations of neuronal NO synthase (nNOS) within the cell. The targeting of nNOS is mediated by adapter proteins that interact with its PDZ domain. Here, we show that the nNOS adapter protein, CAPON, interacts with synapsins I, II, and III through an N-terminal phosphotyrosine-binding domain interaction, which leads to a ternary complex comprising nNOS, CAPON, and synapsin I. The significance of this ternary complex is demonstrated by changes in subcellular localization of nNOS in mice harboring genomic deletions of both synapsin I and synapsin II. These results suggest a mechanism for specific actions of NO at presynaptic sites.

publication date

  • March 5, 2002

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC122496

Digital Object Identifier (DOI)

  • 10.1073/pnas.261705799

PubMed ID

  • 11867766

Additional Document Info

start page

  • 3199

end page

  • 204

volume

  • 99

number

  • 5