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International Journal of Cell Biology
Volume 2014, Article ID 428764, 10 pages
Review Article

S-Nitrosation and Ubiquitin-Proteasome System Interplay in Neuromuscular Disorders

1Department of Biology, University of Rome “Tor Vergata”, 00133 Rome, Italy
2Research Center, IRCCS San Raffaele Pisana, 00166 Rome, Italy

Received 24 May 2013; Revised 18 November 2013; Accepted 21 November 2013; Published 30 January 2014

Academic Editor: Alessio Cardinale

Copyright © 2014 Salvatore Rizza et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Protein S-nitrosation is deemed as a prototype of posttranslational modifications governing cell signaling. It takes place on specific cysteine residues that covalently incorporate a nitric oxide (NO) moiety to form S-nitrosothiol derivatives and depends on the ratio between NO produced by NO synthases and nitrosothiol removal catalyzed by denitrosating enzymes. A large number of cysteine-containing proteins are found to undergo S-nitrosation and, among them, the enzymes catalyzing ubiquitination, mainly the class of ubiquitin E3 ligases and the 20S component of the proteasome, have been reported to be redox modulated in their activity. In this review we will outline the processes regulating S-nitrosation and try to debate whether and how it affects protein ubiquitination and degradation via the proteasome. In particular, since muscle and neuronal health largely depends on the balance between protein synthesis and breakdown, here we will discuss the impact of S-nitrosation in the efficiency of protein quality control system, providing lines of evidence and speculating about its involvement in the onset and maintenance of neuromuscular dysfunctions.