eNOS activation and NO function: Structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity
- Ruslan Rafikov,
- Fabio V Fonseca1,
- Sanjiv Kumar,
- Daniel Pardo,
- Charles Darragh,
- Shawn Elms,
- David Fulton and
- Stephen M Black
- Pulmonary Vascular Disease Program, Vascular Biology Center: CB-3211B, Georgia Health Sciences University, 1459 Laney Walker Boulevard, Augusta, Georgia 30912,
USA
1Department of Cell Biology, Cleveland Clinic, Cleveland, Ohio 44106, USA
- (Correspondence should be addressed to S M Black; Email: sblack{at}georgiahealth.edu)
Abstract
Rather than being a constitutive enzyme as was 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’.
- Received in final form 26 May 2011
- Accepted 3 June 2011
- Made available online as an Accepted Preprint 3 June 2011
- © 2011 Society for Endocrinology
