eNOS activation and NO function: Structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity

Ruslan Rafikov, Fabio V. Fonseca, Sanjiv Kumar, Daniel Pardo, Charles Darragh, Shawn Elms, David Fulton, Stephen M. Black

Research output: Contribution to journalArticle

137 Scopus citations

Abstract

Rather than being a constitutive enzyme aswas first suggested, endothelial nitric oxide synthase (eNOS) is dynamically regulated at the transcriptional, posttranscriptional, and posttranslational levels. This review will focus on how changes in eNOS function are conferred by various posttranslational modifications. The latest knowledge regarding eNOS targeting to the plasma membrane will be discussed as the role of protein phosphorylation as a modulator of catalytic activity. Furthermore, new data are presented that provide novel insights into how disruption of the eNOS dimer prevents eNOS uncoupling and the production of superoxide under conditions of elevated oxidative stress and identifies a novel regulatory region we have termed the 'flexible arm'.

Original languageEnglish (US)
Pages (from-to)271-284
Number of pages14
JournalJournal of Endocrinology
Volume210
Issue number3
DOIs
StatePublished - Sep 2011

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Endocrinology

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