S-Nitrosation and Ubiquitin-Proteasome System Interplay in Neuromuscular Disorders
Joint Authors
Filomeni, Giuseppe
Di Giacomo, Giuseppina
Cirotti, Claudia
Rizza, Salvatore
Montagna, Costanza
Source
International Journal of Cell Biology
Issue
Vol. 2014, Issue 2014 (31 Dec. 2014), pp.1-10, 10 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2014-01-30
Country of Publication
Egypt
No. of Pages
10
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Rizza, Salvatore& Montagna, Costanza& Di Giacomo, Giuseppina& Cirotti, Claudia& Filomeni, Giuseppe. 2014. S-Nitrosation and Ubiquitin-Proteasome System Interplay in Neuromuscular Disorders. International Journal of Cell Biology،Vol. 2014, no. 2014, pp.1-10.
https://search.emarefa.net/detail/BIM-471514
Modern Language Association (MLA)
Rizza, Salvatore…[et al.]. S-Nitrosation and Ubiquitin-Proteasome System Interplay in Neuromuscular Disorders. International Journal of Cell Biology No. 2014 (2014), pp.1-10.
https://search.emarefa.net/detail/BIM-471514
American Medical Association (AMA)
Rizza, Salvatore& Montagna, Costanza& Di Giacomo, Giuseppina& Cirotti, Claudia& Filomeni, Giuseppe. S-Nitrosation and Ubiquitin-Proteasome System Interplay in Neuromuscular Disorders. International Journal of Cell Biology. 2014. Vol. 2014, no. 2014, pp.1-10.
https://search.emarefa.net/detail/BIM-471514
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-471514