Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?

Significance: 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,...

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Autores: Martínez Ruiz, Antonio, Araújo, Inês M., Izquierdo-Álvarez, Alicia, Hernansanz-Agustín, Pablo, Lamas, Santiago, Serrador, Juan M.
Formato: artículo
Fecha de publicación:2013
País:España
Recursos:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/104282
Acesso em linha:https://hdl.handle.net/20.500.14352/104282
Access Level:acceso abierto
Palavra-chave:577.1
577.2
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
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spelling Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?Martínez Ruiz, AntonioAraújo, Inês M.Izquierdo-Álvarez, AliciaHernansanz-Agustín, PabloLamas, SantiagoSerrador, Juan M.577.1577.2Bioquímica (Farmacia)Biología molecular (Farmacia)2302 BioquímicaSignificance: 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.Universidad Complutense de Madrid20132013-10-1020132013-10-10journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/104282reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)InglésengMinisterio de Sanidad y Consumo Not available CP07%2F00143 CP07%2F00143Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 Not available PS09%2F00101 PAPEL DE LAS ESPECIES REACTIVAS DE OXIGENO Y NITROGENO Y DE LAS MODIFICACIONES OXIDATIVAS DE PROTEINAS EN LA RESPUESTA A HIPOXIA EN FISIOPATOLOGIA CARDIOVASCULARMinisterio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 Not available PS09%2F00101 PAPEL DE LAS ESPECIES REACTIVAS DE OXIGENO Y NITROGENO Y DE LAS MODIFICACIONES OXIDATIVAS DE PROTEINAS EN LA RESPUESTA A HIPOXIA EN FISIOPATOLOGIA CARDIOVASCULARopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/1042822026-06-02T12:44:21Z
dc.title.none.fl_str_mv Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
title Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
spellingShingle Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
Martínez Ruiz, Antonio
577.1
577.2
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
title_short Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
title_full Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
title_fullStr Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
title_full_unstemmed Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
title_sort Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
dc.creator.none.fl_str_mv Martínez Ruiz, Antonio
Araújo, Inês M.
Izquierdo-Álvarez, Alicia
Hernansanz-Agustín, Pablo
Lamas, Santiago
Serrador, Juan M.
author Martínez Ruiz, Antonio
author_facet Martínez Ruiz, Antonio
Araújo, Inês M.
Izquierdo-Álvarez, Alicia
Hernansanz-Agustín, Pablo
Lamas, Santiago
Serrador, Juan M.
author_role author
author2 Araújo, Inês M.
Izquierdo-Álvarez, Alicia
Hernansanz-Agustín, Pablo
Lamas, Santiago
Serrador, Juan M.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
577.2
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
topic 577.1
577.2
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
description Significance: 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.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-10-10
2013
2013-10-10
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/104282
url https://hdl.handle.net/20.500.14352/104282
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Sanidad y Consumo Not available CP07%2F00143 CP07%2F00143
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 Not available PS09%2F00101 PAPEL DE LAS ESPECIES REACTIVAS DE OXIGENO Y NITROGENO Y DE LAS MODIFICACIONES OXIDATIVAS DE PROTEINAS EN LA RESPUESTA A HIPOXIA EN FISIOPATOLOGIA CARDIOVASCULAR
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 Not available PS09%2F00101 PAPEL DE LAS ESPECIES REACTIVAS DE OXIGENO Y NITROGENO Y DE LAS MODIFICACIONES OXIDATIVAS DE PROTEINAS EN LA RESPUESTA A HIPOXIA EN FISIOPATOLOGIA CARDIOVASCULAR
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301603

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