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Specificity in S-Nitrosylation: a short-range mechanism for NO signaling?

2013-10Journal article Open Access
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dc.contributor.authorMartinez-Ruiz, Antonio
dc.contributor.authorAraújo, Inês
dc.contributor.authorIzquierdo-Alvarez, Alicia
dc.contributor.authorHernansanz-Agustin, Pablo
dc.contributor.authorLamas, Santiago
dc.contributor.authorSerrador, Juan M.
dc.date.accessioned2018-12-07T14:58:06Z
dc.date.available2018-12-07T14:58:06Z
dc.date.issued2013-10
dc.description.abstractSignificance: Nitric oxide (NO) classical and less classical signaling mechanisms (through interaction with soluble guanylate cyclase and cytochrome c oxidase, respectively) operate through direct binding of NO to protein metal centers, and rely on diffusibility of the NO molecule. S-Nitrosylation, a covalent post-translational modification of protein cysteines, has emerged as a paradigm of nonclassical NO signaling. Recent Advances: Several nonenzymatic mechanisms for S-nitrosylation formation and destruction have been described. Enzymatic mechanisms for transnitrosylation and denitrosylation have been also studied as regulators of the modification of specific subsets of proteins. The advancement of modification-specific proteomic methodologies has allowed progress in the study of diverse S-nitrosoproteomes, raising clues and questions about the parameters for determining the protein specificity of the modification. Critical Issues: We propose that S-nitrosylation is mainly a short-range mechanism of NO signaling, exerted in a relatively limited range of action around the NO sources, and tightly related to the very controlled regulation of subcellular localization of nitric oxide synthases. We review the nonenzymatic and enzymatic mechanisms that support this concept, as well as physiological examples of mammalian systems that illustrate well the precise compartmentalization of S-nitrosylation. Future Directions: Individual and proteomic studies of protein S-nitrosylation-based signaling should take into account the subcellular localization in order to gain further insight into the functional role of this modification in (patho)physiological settings. Antioxid. Redox Signal. 19, 1220-1235.
dc.description.sponsorshipSpanish Government [CSD2007-00020, CP07/00143, PS09/00101, SAF2009-7520, PI10/02136]; Spanish-Portuguese Integrated Action Grant [PRI-AIBPT-2011-1015/E-10/12]; Foundation for Science and Technology (FCT, Portugal) [PTDC/SAU-NEU/102612/2008, PTDC/SAU-NMC/112183/2009, PEst-OE/EQB/LA0023/2011]; COST action [BM1005]
dc.description.versioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doi10.1089/ars.2012.5066
dc.identifier.issn1523-0864
dc.identifier.issn1557-7716
dc.identifier.urihttp://hdl.handle.net/10400.1/11864
dc.language.isoeng
dc.peerreviewedyes
dc.publisherMary Ann Liebert, Inc
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectNitric-oxide synthase
dc.subjectProtein-tyrosine nitration
dc.subjectVascular endothelial-cells
dc.subjectEnos-derived no
dc.subjectRed-blood-cells
dc.subjectNmda receptor
dc.subjectMolecular-mechanisms
dc.subjectRelaxing factor
dc.subjectDinitrosyliron complexes
dc.subjectSpatial confinement
dc.titleSpecificity in S-Nitrosylation: a short-range mechanism for NO signaling?
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage1235
oaire.citation.issue11
oaire.citation.startPage1220
oaire.citation.titleAntioxidants and Redox Signaling
oaire.citation.volume19
person.familyNamePombinho de Araújo
person.givenNameInês Maria
person.identifierF-4703-2012
person.identifier.ciencia-idD11F-D4CA-2947
person.identifier.orcid0000-0002-2438-0111
person.identifier.scopus-author-id56271084100
rcaap.rightsrestrictedAccess
rcaap.typearticle
relation.isAuthorOfPublication1d0c21f4-0f4b-4589-8412-fe1079419774
relation.isAuthorOfPublication.latestForDiscovery1d0c21f4-0f4b-4589-8412-fe1079419774

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