ReviewNO Means No and Yes: Regulation of Cell Signaling by Protein Nitrosylation

@article{Mannick2004ReviewNOMN,
  title={ReviewNO Means No and Yes: Regulation of Cell Signaling by Protein Nitrosylation},
  author={Joan B. Mannick and Christopher M Schonhoff},
  journal={Free Radical Research},
  year={2004},
  volume={38},
  pages={1 - 7}
}
Protein nitrosylation is emerging as a key mechanism by which nitric oxide regulates cell signaling. Nitrosylation is the binding of a NO group to a metal or thiol (-SH) on a peptide or protein. Like phosphorylation, nitrosylation is a precisely targeted and rapidly reversible posttranslational modification that allows cells to flexibly and specifically respond to changes in their environment. An increasing number of proteins have been identified whose activity is regulated by intracellular… 
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References

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TLDR
Protein S-nitrosylation is established as a physiological signalling mechanism for neuronally generated NO in mice harbouring a genomic deletion of neuronal NO synthase (nNOS).
S-Nitrosylation Is Emerging as a Specific and Fundamental Posttranslational Protein Modification: Head-to-Head Comparison with O-Phosphorylation
TLDR
A head-to-head comparison suggests that S-nitrosylation, like O-phosphorylation, may similarly play a fundamental role in the post-translational control of protein activity and cellular function.
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TLDR
This review surveys what the authors believe to be the most important mechanisms and targets of signaling by NO.
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TLDR
Nitrosylation may provide a broad-based mechanism for regulating interactions between proteins, and systematic proteomic analyses in which redox state and NO bioavailability are carefully controlled will reveal a large array of novel interactions.
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TLDR
These results, which demonstrate Ca2+, neurohumoral, growth factor, cytokine, and developmental regulation of protein S-nitrosylation that is coupled to NOS expression and activity, provide unique evidence for the proposition that this ubiquitous NO-derived post-translational protein modification serves as a major effector of NO-related bioactivity.
Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
Thioredoxin 1 (Trx) is a known redox regulator that is implicated in the redox control of cell growth and apoptosis inhibition. Here we show that Trx is essential for maintaining the content of
Nitrosylation The Prototypic Redox-Based Signaling Mechanism
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TLDR
Protein S-nitrosylated/denitrosylation can thus serve as a regulatory process in signal transduction pathways.
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TLDR
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