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Article

Subcellular targeting and agonist-induced site-specific phosphorylation of endothelial nitric-oxide synthase.

The Journal of biological chemistry - 18 Oct 2002

Gonzalez Eva, Kou Ruqin, Lin Alison J, Golan David E, Michel Thomas

Abstract excerpt

The endothelial isoform of nitric-oxide synthase (eNOS) undergoes a complex pattern of covalent modifications, including acylation with the fatty acids myristate and palmitate as well as phosphorylation on multiple sites. eNOS acylation is a key determinant for the reversible subcellular targeting of the enzyme to plasmalemmal caveolae. We transfected a series of hemagglutinin epitope-tagged eNOS mutant cDNAs...

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Identifiers

PMID: 12189156
DOI: 10.1074/jbc.M207299200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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