Cited by 125Nitric Oxide and Endothelin EffectsRedox biology and oxidative stressReceptor Mechanisms and Signaling

Subcellular targeting and trafficking of nitric oxide synthases

Open access
Oess, Stefanie, Icking, Ann, Fulton, David, Govers, Roland, Müller-Esterl, Werner·2006·Biochemical Journal

Abstract

Unlike most other endogenous messengers that are deposited in vesicles, processed on demand and/or secreted in a regulated fashion, NO (nitric oxide) is a highly active molecule that readily diffuses through cell membranes and thus cannot be stored inside the producing cell. Rather, its signalling capacity must be controlled at the levels of biosynthesis and local availability. The importance of temporal and spatial control of NO production is highlighted by the finding that differential localization of NO synthases in cardiomyocytes translates into distinct effects of NO in the heart. Thus NO synthases belong to the most tightly controlled enzymes, being regulated at transcriptional and translational levels, through co- and post-translational modifications, by substrate availability and not least via specific sorting to subcellular compartments, where they are in close proximity to their target proteins. Considerable efforts have been made to elucidate the molecular mechanisms that underlie the intracellular targeting and trafficking of NO synthases, to ultimately understand the cellular pathways controlling the formation and function of this powerful signalling molecule. In the present review, we discuss the mechanisms and triggers for subcellular routing and dynamic redistribution of NO synthases and the ensuing consequences for NO production and action.

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  • eNOS location in the cell and activity are controlled by Ca2+ and calmodulin.

    “Its location in the cell and activity are controlled by Ca2+ and calmodulin, as well as post-translational modifications such as phosphorylation and myristoylation (29, 30).”
  • eNOS location and activity are controlled by post-translational modifications such as phosphorylation and myristoylation.

    “Its location in the cell and activity are controlled by Ca2+ and calmodulin, as well as post-translational modifications such as phosphorylation and myristoylation (29, 30).”
  • The iNOS and nNOS isoforms are soluble and predominantly found in the cytosol, while eNOS is membrane-associated.

    “The iNOS and nNOS isoforms are soluble and predominantly they are found in the cytosol, while eNOS is membrane-associated [108].”

    From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [108]

  • NOS3 produces relatively low quantities of NO, and its activity is controlled by calcium/calmodulin, post-translational modifications, and physical forces such as shear stress.

    “It produces relatively low quantities of NO, and its activity is controlled by Ca2+ and calmodulin, post-translational modifications [72, 73], and physical forces such as shear stress [74, 75].”

    From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [72]

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Authors
Oess, S., Icking, A., Fulton, D., Govers, R., & Müller-Esterl, W.
Affiliations
  • Goethe University Frankfurt (DE)
  • Augusta University (US)
  • Inserm (FR)
  • Institute of Biochemistry II, University of Frankfurt Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany
Corresponding author
  • Oess, Stefanie
  • Icking, Ann
Venue
Biochemical Journal
Published
2006-05-29
Volume
396
Issue
3
Pages
401-409
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W2163693604
Cited by
125
References
124
Citations by year
2026: 1 · 2025: 2 · 2024: 2 · 2022: 1 · 2021: 4 · 2020: 1 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 6 · 2015: 4 · 2014: 11 · 2013: 6 · 2012: 18
FWCI
1.20
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL AMU (submittedVersion)
Funders
Nederlandse Organisatie voor Wetenschappelijk Onderzoek (902-26-224)
Topics
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
nitric oxide synthase, subcellular targeting, protein trafficking, nitric oxide signaling, cardiomyocytes, post-translational modification, protein sorting
MeSH terms
Acylation, Animals, Humans, Subcellular Fractions, Nitric Oxide Synthase, Protein Transport, Nitric Oxide Synthase Type I, Nitric Oxide Synthase Type III

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