Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON.
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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acids, Animals, Binding Sites, Brain, Carrier Proteins, Mice, Mice, Knockout, Neurons, Nitric Oxide Synthase, Nitric Oxide Synthase Type I, Protein Structure, Tertiary, Subcellular Fractions, Synapsins
Adaptor Proteins, Signal Transducing, Amino Acids, Animals, Binding Sites, Brain, Carrier Proteins, Mice, Mice, Knockout, Neurons, Nitric Oxide Synthase, Nitric Oxide Synthase Type I, Protein Structure, Tertiary, Subcellular Fractions, Synapsins
Proc. Natl. Acad. Sci. U.S.A.
Date: Mar. 05, 2002
PubMed ID: 11867766
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