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

  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},
  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… 
S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration[W][OA]
It is concluded that NO regulates the effects of its own radicals through the S-nitrosylation of crucial components of the antioxidant defense system that function as common triggers for reactive oxygen species– and NO-mediated signaling events.
Metacaspase Activity of Arabidopsis thaliana Is Regulated by S-Nitrosylation of a Critical Cysteine Residue*
S-nitrosylation plays a central role in the regulation of the proteolytic activity of Arabidopsis thaliana metacaspase 9 (AtMC9) and it is found that AtMC9 zymogens are S-Nitrosylated at their active site cysteines in vivo and that this posttranslational modification suppresses both At MC9 autoprocessing and proteolytics activity.
Nitric Oxide and Reactive Nitrogen Species
Nitric oxide (NO) plays a key role in plant metabolism, signaling, defense, and development. However, a fundamental question arises how the NO message is converted into a physiological response.
Nitric oxide-mediated signaling in pulmonary endothelial cells
The laboratory has focused on S-nitrosation of the metal binding protein metallothionein and the resulting effects on zinc homeostasis, gene and protein expression and nitric oxide mediated signaling in the pulmonary endothelium, and identified several potential targets of S-Nitrosation in endothelial cells including cytoskeletal, cytoprotective, glycolytic and chaperone proteins.
S-nitrosation versus S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione.
Results show that papain, creatine phosphokinase, and glyceraldehyde-3-phosphate dehydrogenase were significantly both S-nitrosated and S-glutathionylated by GSNO, whereas alcohol dehydrogenases, bovine serum albumin, and actin appeared nearly only S-Nitrosated.
Proteomic analysis of S‐nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response
By using a proteomic approach involving 2‐DE and MS, changes in S‐nitrosylated proteins in Arabidopsis thaliana undergoing HR are characterized, for the first time, and the 16 proteins identified are mostly enzymes serving intermediary metabolism, signaling and antioxidant defense.
Salinity-induced changes in S-nitrosylation of pea mitochondrial proteins.
Nitric Oxide Signaling System in Plant Innate Immunity
Nitric oxide (NO) is a diffusible molecular messenger that plays an important role in plant immune response signal transduction and is a key regulator of protein function in plant immunity.


Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
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
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.
Cell signaling by nitric oxide.
This review surveys what the authors believe to be the most important mechanisms and targets of signaling by NO.
Screening for Nitric Oxide-Dependent Protein-Protein Interactions
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.
Basal and Stimulated Protein S-Nitrosylation in Multiple Cell Types and Tissues*
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
Fas-induced caspase denitrosylation.
Protein S-nitrosylated/denitrosylation can thus serve as a regulatory process in signal transduction pathways.
Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation
It is shown that the NMDA receptor (NMDAR)-associated ion channel was modulated not only by exogenous NO but also by endogenous NO, and endogenous S-nitrosylation can regulate ion channel activity.