Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON

Samie R. Jaffrey, Fabio Benfenati, Adele M. Snowman, Andrew J. Czernik, Solomon H. Snyder

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)3199-3204
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number5
DOIs
StatePublished - Mar 5 2002

ASJC Scopus subject areas

  • General

Fingerprint

Dive into the research topics of 'Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON'. Together they form a unique fingerprint.

Cite this