Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling.
S-nitrosylase
S-nitrosylation
denitrosylation
nitric oxide
redox signaling
Journal
Antioxidants & redox signaling
ISSN: 1557-7716
Titre abrégé: Antioxid Redox Signal
Pays: United States
ID NLM: 100888899
Informations de publication
Date de publication:
01 04 2019
01 04 2019
Historique:
pubmed:
14
11
2017
medline:
25
6
2020
entrez:
14
11
2017
Statut:
ppublish
Résumé
Protein S-nitrosylation, the oxidative modification of cysteine by nitric oxide (NO) to form protein S-nitrosothiols (SNOs), mediates redox-based signaling that conveys, in large part, the ubiquitous influence of NO on cellular function. S-nitrosylation regulates protein activity, stability, localization, and protein-protein interactions across myriad physiological processes, and aberrant S-nitrosylation is associated with diverse pathophysiologies. Recent Advances: It is recently recognized that S-nitrosylation endows S-nitroso-protein (SNO-proteins) with S-nitrosylase activity, that is, the potential to trans-S-nitrosylate additional proteins, thereby propagating SNO-based signals, analogous to kinase-mediated signaling cascades. In addition, it is increasingly appreciated that cellular S-nitrosylation is governed by dynamically coupled equilibria between SNO-proteins and low-molecular-weight SNOs, which are controlled by a growing set of enzymatic denitrosylases comprising two main classes (high and low molecular weight). S-nitrosylases and denitrosylases, which together control steady-state SNO levels, may be identified with distinct physiology and pathophysiology ranging from cardiovascular and respiratory disorders to neurodegeneration and cancer. The target specificity of protein S-nitrosylation and the stability and reactivity of protein SNOs are determined substantially by enzymatic machinery comprising highly conserved transnitrosylases and denitrosylases. Understanding the differential functionality of SNO-regulatory enzymes is essential, and is amenable to genetic and pharmacological analyses, read out as perturbation of specific equilibria within the SNO circuitry. The emerging picture of NO biology entails equilibria among potentially thousands of different SNOs, governed by denitrosylases and nitrosylases. Thus, to elucidate the operation and consequences of S-nitrosylation in cellular contexts, studies should consider the roles of SNO-proteins as both targets and transducers of S-nitrosylation, functioning according to enzymatically governed equilibria.
Identifiants
pubmed: 29130312
doi: 10.1089/ars.2017.7403
pmc: PMC6391618
doi:
Substances chimiques
Proteins
0
S-Nitrosothiols
0
Nitric Oxide
31C4KY9ESH
Cysteine
K848JZ4886
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1331-1351Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL126900
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007250
Pays : United States
Organisme : NCATS NIH HHS
ID : TL1 TR002549
Pays : United States
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