Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-11768
Nat Neurosci 2000 Jan 01;31:15-21. doi: 10.1038/71090.
Show Gene links Show Anatomy links

Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation.

Choi YB , Tenneti L , Le DA , Ortiz J , Bai G , Chen HS , Lipton SA .


???displayArticle.abstract???
Several ion channels are thought to be directly modulated by nitric oxide (NO), but the molecular basis of this regulation is unclear. Here we show that the NMDA receptor (NMDAR)-associated ion channel was modulated not only by exogenous NO but also by endogenous NO. Site-directed mutagenesis identified a critical cysteine residue (Cys 399) on the NR2A subunit whose S-nitrosylation (NO+ transfer) under physiological conditions underlies this modulation. In cell systems expressing NMDARs with mutant NR2A subunits in which this single cysteine was replaced by an alanine, the effect of endogenous NO was lost. Thus endogenous S-nitrosylation can regulate ion channel activity.

???displayArticle.pubmedLink??? 10607390
???displayArticle.link??? Nat Neurosci
???displayArticle.grants??? [+]

Species referenced: Xenopus laevis
Genes referenced: grin2a