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Article

Calcium/calmodulin-dependent protein kinase I inhibits neuronal nitric-oxide synthase activity through serine 741 phosphorylation.

FEBS letters - 16 Jul 2004

Song Tao, Hatano Naoya, Horii Mariko, Tokumitsu Hiroshi, Yamaguchi Fuminori, Tokuda Masaaki, Watanabe Yasuo

Abstract excerpt

We demonstrate here that neuronal nitric-oxide synthase (nNOS) is phosphorylated and inhibited by a constitutively active form of Ca2+/calmodulin (CaM)-dependent protein kinase I (CaM-K I1-293). Substitution of Ser741 to Ala in nNOS blocked the phosphorylation and the inhibitory effect. Mimicking phosphorylation at Ser741 by Ser to Asp mutation resulted in decreased binding of and activation by CaM, since the...

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Identifiers

PMID: 15251453
DOI: 10.1016/j.febslet.2004.05.083

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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