Lighting up T lymphocyte signaling with quantitative phosphoproteomics

Phosphorylation is the most abundant post-translational modification, regulating several aspects of protein and cell function. Quantitative phosphoproteomics approaches have expanded the scope of phosphorylation analysis enabling the quantification of changes in thousands of phosphorylation sites si...

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Detalles Bibliográficos
Autores: Álvarez-Salamero, Candelas, Castillo-González, Raquel, Navarro, María N.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/166195
Acceso en línea:http://hdl.handle.net/10261/166195
Access Level:acceso abierto
Palabra clave:Phosphoproteomics
Mass-spectrometry
Signaling
Phosphorylation
T lymphocyte
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spelling Lighting up T lymphocyte signaling with quantitative phosphoproteomicsÁlvarez-Salamero, CandelasCastillo-González, RaquelNavarro, María N.PhosphoproteomicsMass-spectrometrySignalingPhosphorylationT lymphocytePhosphorylation is the most abundant post-translational modification, regulating several aspects of protein and cell function. Quantitative phosphoproteomics approaches have expanded the scope of phosphorylation analysis enabling the quantification of changes in thousands of phosphorylation sites simultaneously in two or more conditions. These approaches offer a global view of the impact of cellular perturbations such as extracellular stimuli or gene ablation in intracellular signaling networks. Such great potential also brings on a new challenge: to identify, among the thousands of phosphorylations found in global phosphoproteomics studies, the small subset of site-specific phosphorylations expected to be functionally relevant. This review focus on updating and integrating findings on T lymphocyte signaling generated using global phosphoproteomics approaches, drawing attention on the biological relevance of the obtained data.Spanish Ministry of Economy and Competitiveness Peer ReviewedMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2018201820172018info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/166195reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1661952026-05-22T06:33:51Z
dc.title.none.fl_str_mv Lighting up T lymphocyte signaling with quantitative phosphoproteomics
title Lighting up T lymphocyte signaling with quantitative phosphoproteomics
spellingShingle Lighting up T lymphocyte signaling with quantitative phosphoproteomics
Álvarez-Salamero, Candelas
Phosphoproteomics
Mass-spectrometry
Signaling
Phosphorylation
T lymphocyte
title_short Lighting up T lymphocyte signaling with quantitative phosphoproteomics
title_full Lighting up T lymphocyte signaling with quantitative phosphoproteomics
title_fullStr Lighting up T lymphocyte signaling with quantitative phosphoproteomics
title_full_unstemmed Lighting up T lymphocyte signaling with quantitative phosphoproteomics
title_sort Lighting up T lymphocyte signaling with quantitative phosphoproteomics
dc.creator.none.fl_str_mv Álvarez-Salamero, Candelas
Castillo-González, Raquel
Navarro, María N.
author Álvarez-Salamero, Candelas
author_facet Álvarez-Salamero, Candelas
Castillo-González, Raquel
Navarro, María N.
author_role author
author2 Castillo-González, Raquel
Navarro, María N.
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Phosphoproteomics
Mass-spectrometry
Signaling
Phosphorylation
T lymphocyte
topic Phosphoproteomics
Mass-spectrometry
Signaling
Phosphorylation
T lymphocyte
description Phosphorylation is the most abundant post-translational modification, regulating several aspects of protein and cell function. Quantitative phosphoproteomics approaches have expanded the scope of phosphorylation analysis enabling the quantification of changes in thousands of phosphorylation sites simultaneously in two or more conditions. These approaches offer a global view of the impact of cellular perturbations such as extracellular stimuli or gene ablation in intracellular signaling networks. Such great potential also brings on a new challenge: to identify, among the thousands of phosphorylations found in global phosphoproteomics studies, the small subset of site-specific phosphorylations expected to be functionally relevant. This review focus on updating and integrating findings on T lymphocyte signaling generated using global phosphoproteomics approaches, drawing attention on the biological relevance of the obtained data.
publishDate 2017
dc.date.none.fl_str_mv 2017
2018
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/166195
url http://hdl.handle.net/10261/166195
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,81155

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