title: S-Nitrosylation in neurogenesis and neuronal development.
abstract: BACKGROUND
  Nitric oxide (NO) is a pleiotropic messenger molecule. The multidimensional actions of NO species are, in part, mediated by their redox nature. Oxidative posttranslational modification of cysteine residues to regulate protein function, termed S-nitrosylation, constitutes a major form of redox-based signaling by NO.
  
  
  METHODS
  S-Nitrosylation directly modifies a number of cytoplasmic and nuclear proteins in neurons. S-Nitrosylation modulates neuronal development by reaction with specific proteins, including the transcription factor MEF2. This review focuses on the impact of S-nitrosylation on neurogenesis and neuronal development.
  
  
  CONCLUSIONS
  Functional characterization of S-nitrosylated proteins that regulate neuronal development represents a rapidly emerging field. Recent studies reveal that S-nitrosylation-mediated redox signaling plays an important role in several biological processes essential for neuronal differentiation and maturation.
  
  
  CONCLUSIONS
  Investigation of S-nitrosylation in the nervous system has elucidated new molecular and cellular mechanisms for neuronal development. S-Nitrosylated proteins in signaling networks modulate key events in brain development. Dysregulation of this redox-signaling pathway may contribute to neurodevelopmental disabilities such as autism spectrum disorder (ASD). Thus, further elucidation of the involvement of S-nitrosylation in brain development may offer potential therapeutic avenues for neurodevelopmental disorders. This article is part of a Special Issue entitled Redox regulation of differentiation and de-differentiation.
authors.affiliation: Neuroscience and Aging Research Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA; Department of Neurosciences, University of California San Diego, School of Medicine, 9500 Gilman Drive, La Jolla, CA, USA. Electronic address: sokamoto@sbmri.org.
authors.forename: Shu-ichi
authors.initials: S
authors.lastname: Okamoto
authors.affiliation: Neuroscience and Aging Research Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA; Department of Neurosciences, University of California San Diego, School of Medicine, 9500 Gilman Drive, La Jolla, CA, USA. Electronic address: slipton@ucsd.edu.
authors.forename: Stuart A
authors.initials: SA
authors.lastname: Lipton
mesh_terms: D001921:Brain / Q000166:cytology / Q000254:growth & development / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D006801:Humans; D008959:Models, Neurological; D055495:Neurogenesis; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D009569:Nitric Oxide / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D014157:Transcription Factors; D009569:Nitric Oxide; D003545:Cysteine
keywords: CREB; MEF2; Neurodevelopmental disorder; Nitric oxide; Redox signaling; S-Nitrosylation