Subcellular targeting and trafficking of nitric oxide synthases
Open accessAbstract
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).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [29]
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).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [29]
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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What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology
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Regulation of obesity and insulin resistance by nitric oxide
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“It produces relatively low quantities of NO, and its activity is controlled by Ca2þ and calmodulin, posttranslational modifications [72,73], and physical forces such as shear stress [74,75].”
BackgroundEndothelial nitric oxide (NO) and its pathophysiologic regulation
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The Role of Reactive Species on Innate Immunity
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The ubiquitin E3 ligase NOSIP modulates protein phosphatase 2A activity in craniofacial development
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Self-citation
- 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
- Publisher
- Portland Press Ltd.
- Published
- 2006-05-29
- Volume
- 396
- Issue
- 3
- Pages
- 401-409
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1482820
- 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
- bronze
- doi.org
- 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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