Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis

Global analysis of protein phosphorylation by mass spectrometry proteomic techniques has emerged in the last decades as a powerful tool in biological and biomedical research. However, there are several factors that make the global study of the phosphoproteome more challenging than measuring non-modi...

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Autores: Colomé, Núria, Abian, Joaquín, Aloria, Kerman, Arizmendi, Jesús M., Barceló-Batllori, Silvia, Braga-Lagache, Sophie, Burlet-Schiltz, Odile, Carrascal, Montse, Casal, Ignacio J., Chicano-Gálvez, Eduard, Chiva, Cristina, Clemente, Luis F., Elortza, Félix, Estanyol, Josep M., Fernández Irigoyen, Joaquín, Fernández-Puente, Patricia, Fidalgo, María J., Froment, Carine, Fuentes, Manuel, Fuentes-Almagro, Carlos, Gay, Marina, Hainard, Alexandre, Heller, Manfred, Hernández, María Luisa, Ibarrola, Nieves, Iloro, Ibon, Kieselbach, Thomas, Lario, Antonio, Locard-Paulet, Marie, Marina-Ramírez, Anabel, Martín, Luna, Morato-López, Esperanza, Muñoz, Javier, Navajas, Rosana, Odena, Antonia M., Odriozola, Leticia, Oliveira, Eliandre de, Paradela, Alberto, Pasquarello, Carla, Rios, Vivian de los, Ruiz-Romero, Cristina, Sabidó, Eduard, Sánchez del Pino, Manuel, Sancho, Jaime, Santamaría Martínez, Enrique, Schaeffer-Reiss, Christine, Schneider, Justine, Torre, Carolina de la, Valero, Luz M., Vilaseca, Marta, Wu, Shuai, Wu, Linfeng, Ximénez de Embún, Pilar, Canals, Francesc, Corrales, Fernando J., ProteoRed-ISCIII, EuPA
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Recursos:Universidad Pública de Navarra
Repositorio:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
OAI Identifier:oai:academica-e.unavarra.es:2454/42711
Acesso em linha:https://hdl.handle.net/2454/42711
Access Level:acceso abierto
Palavra-chave:Phosphoproteome
Mass-spectrometry
Proteomics
Experiment
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spelling Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysisColomé, NúriaAbian, JoaquínAloria, KermanArizmendi, Jesús M.Barceló-Batllori, SilviaBraga-Lagache, SophieBurlet-Schiltz, OdileCarrascal, MontseCasal, Ignacio J.Chicano-Gálvez, EduardChiva, CristinaClemente, Luis F.Elortza, FélixEstanyol, Josep M.Fernández Irigoyen, JoaquínFernández-Puente, PatriciaFidalgo, María J.Froment, CarineFuentes, ManuelFuentes-Almagro, CarlosGay, MarinaHainard, AlexandreHeller, ManfredHernández, María LuisaIbarrola, NievesIloro, IbonKieselbach, ThomasLario, AntonioLocard-Paulet, MarieMarina-Ramírez, AnabelMartín, LunaMorato-López, EsperanzaMuñoz, JavierNavajas, RosanaOdena, Antonia M.Odriozola, LeticiaOliveira, Eliandre deParadela, AlbertoPasquarello, CarlaRios, Vivian de losRuiz-Romero, CristinaSabidó, EduardSánchez del Pino, ManuelSancho, JaimeSantamaría Martínez, EnriqueSchaeffer-Reiss, ChristineSchneider, JustineTorre, Carolina de laValero, Luz M.Vilaseca, MartaWu, ShuaiWu, LinfengXiménez de Embún, PilarCanals, FrancescCorrales, Fernando J.ProteoRed-ISCIIIEuPAPhosphoproteomeMass-spectrometryProteomicsExperimentGlobal analysis of protein phosphorylation by mass spectrometry proteomic techniques has emerged in the last decades as a powerful tool in biological and biomedical research. However, there are several factors that make the global study of the phosphoproteome more challenging than measuring non-modified proteins. The low stoichiometry of the phosphorylated species and the need to retrieve residue specific information require particular attention on sample preparation, data acquisition and processing to ensure reproducibility, qualitative and quantitative robustness and ample phosphoproteome coverage in phosphoproteomic workflows. Aiming to investigate the effect of different variables in the performance of proteome wide phosphoprotein analysis protocols, ProteoRed-ISCIII and EuPA launched the Proteomics Multicentric Experiment 11 (PME11). A reference sample consisting of a yeast protein extract spiked in with different amounts of a phosphomix standard (Sigma/Merck) was distributed to 31 laboratories around the globe. Thirty-six datasets from 23 laboratories were analyzed. Our results indicate the suitability of the PME11 reference sample to benchmark and optimize phosphoproteomics strategies, weighing the influence of different factors, as well as to rank intra and inter laboratory performance.ProteoRed, PRB3 is supported by grant PT17/0019/0001 , of the PE I+D+i 2013-2016 , funded by ISCIII and ERDF.ElsevierCiencias de la SaludOsasun Zientziak2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/ziphttps://hdl.handle.net/2454/42711reponame:Academica-e. Repositorio Institucional de la Universidad Pública de Navarrainstname:Universidad Pública de NavarraInglés© 2021 The Authors. Creative Commons Attribution 4.0 Internationalhttps://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:academica-e.unavarra.es:2454/427112026-06-17T12:41:47Z
dc.title.none.fl_str_mv Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
spellingShingle Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
Colomé, Núria
Phosphoproteome
Mass-spectrometry
Proteomics
Experiment
title_short Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_full Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_fullStr Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_full_unstemmed Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_sort Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
dc.creator.none.fl_str_mv Colomé, Núria
Abian, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló-Batllori, Silvia
Braga-Lagache, Sophie
Burlet-Schiltz, Odile
Carrascal, Montse
Casal, Ignacio J.
Chicano-Gálvez, Eduard
Chiva, Cristina
Clemente, Luis F.
Elortza, Félix
Estanyol, Josep M.
Fernández Irigoyen, Joaquín
Fernández-Puente, Patricia
Fidalgo, María J.
Froment, Carine
Fuentes, Manuel
Fuentes-Almagro, Carlos
Gay, Marina
Hainard, Alexandre
Heller, Manfred
Hernández, María Luisa
Ibarrola, Nieves
Iloro, Ibon
Kieselbach, Thomas
Lario, Antonio
Locard-Paulet, Marie
Marina-Ramírez, Anabel
Martín, Luna
Morato-López, Esperanza
Muñoz, Javier
Navajas, Rosana
Odena, Antonia M.
Odriozola, Leticia
Oliveira, Eliandre de
Paradela, Alberto
Pasquarello, Carla
Rios, Vivian de los
Ruiz-Romero, Cristina
Sabidó, Eduard
Sánchez del Pino, Manuel
Sancho, Jaime
Santamaría Martínez, Enrique
Schaeffer-Reiss, Christine
Schneider, Justine
Torre, Carolina de la
Valero, Luz M.
Vilaseca, Marta
Wu, Shuai
Wu, Linfeng
Ximénez de Embún, Pilar
Canals, Francesc
Corrales, Fernando J.
ProteoRed-ISCIII
EuPA
author Colomé, Núria
author_facet Colomé, Núria
Abian, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló-Batllori, Silvia
Braga-Lagache, Sophie
Burlet-Schiltz, Odile
Carrascal, Montse
Casal, Ignacio J.
Chicano-Gálvez, Eduard
Chiva, Cristina
Clemente, Luis F.
Elortza, Félix
Estanyol, Josep M.
Fernández Irigoyen, Joaquín
Fernández-Puente, Patricia
Fidalgo, María J.
Froment, Carine
Fuentes, Manuel
Fuentes-Almagro, Carlos
Gay, Marina
Hainard, Alexandre
Heller, Manfred
Hernández, María Luisa
Ibarrola, Nieves
Iloro, Ibon
Kieselbach, Thomas
Lario, Antonio
Locard-Paulet, Marie
Marina-Ramírez, Anabel
Martín, Luna
Morato-López, Esperanza
Muñoz, Javier
Navajas, Rosana
Odena, Antonia M.
Odriozola, Leticia
Oliveira, Eliandre de
Paradela, Alberto
Pasquarello, Carla
Rios, Vivian de los
Ruiz-Romero, Cristina
Sabidó, Eduard
Sánchez del Pino, Manuel
Sancho, Jaime
Santamaría Martínez, Enrique
Schaeffer-Reiss, Christine
Schneider, Justine
Torre, Carolina de la
Valero, Luz M.
Vilaseca, Marta
Wu, Shuai
Wu, Linfeng
Ximénez de Embún, Pilar
Canals, Francesc
Corrales, Fernando J.
ProteoRed-ISCIII
EuPA
author_role author
author2 Abian, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló-Batllori, Silvia
Braga-Lagache, Sophie
Burlet-Schiltz, Odile
Carrascal, Montse
Casal, Ignacio J.
Chicano-Gálvez, Eduard
Chiva, Cristina
Clemente, Luis F.
Elortza, Félix
Estanyol, Josep M.
Fernández Irigoyen, Joaquín
Fernández-Puente, Patricia
Fidalgo, María J.
Froment, Carine
Fuentes, Manuel
Fuentes-Almagro, Carlos
Gay, Marina
Hainard, Alexandre
Heller, Manfred
Hernández, María Luisa
Ibarrola, Nieves
Iloro, Ibon
Kieselbach, Thomas
Lario, Antonio
Locard-Paulet, Marie
Marina-Ramírez, Anabel
Martín, Luna
Morato-López, Esperanza
Muñoz, Javier
Navajas, Rosana
Odena, Antonia M.
Odriozola, Leticia
Oliveira, Eliandre de
Paradela, Alberto
Pasquarello, Carla
Rios, Vivian de los
Ruiz-Romero, Cristina
Sabidó, Eduard
Sánchez del Pino, Manuel
Sancho, Jaime
Santamaría Martínez, Enrique
Schaeffer-Reiss, Christine
Schneider, Justine
Torre, Carolina de la
Valero, Luz M.
Vilaseca, Marta
Wu, Shuai
Wu, Linfeng
Ximénez de Embún, Pilar
Canals, Francesc
Corrales, Fernando J.
ProteoRed-ISCIII
EuPA
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dc.contributor.none.fl_str_mv Ciencias de la Salud
Osasun Zientziak
dc.subject.none.fl_str_mv Phosphoproteome
Mass-spectrometry
Proteomics
Experiment
topic Phosphoproteome
Mass-spectrometry
Proteomics
Experiment
description Global analysis of protein phosphorylation by mass spectrometry proteomic techniques has emerged in the last decades as a powerful tool in biological and biomedical research. However, there are several factors that make the global study of the phosphoproteome more challenging than measuring non-modified proteins. The low stoichiometry of the phosphorylated species and the need to retrieve residue specific information require particular attention on sample preparation, data acquisition and processing to ensure reproducibility, qualitative and quantitative robustness and ample phosphoproteome coverage in phosphoproteomic workflows. Aiming to investigate the effect of different variables in the performance of proteome wide phosphoprotein analysis protocols, ProteoRed-ISCIII and EuPA launched the Proteomics Multicentric Experiment 11 (PME11). A reference sample consisting of a yeast protein extract spiked in with different amounts of a phosphomix standard (Sigma/Merck) was distributed to 31 laboratories around the globe. Thirty-six datasets from 23 laboratories were analyzed. Our results indicate the suitability of the PME11 reference sample to benchmark and optimize phosphoproteomics strategies, weighing the influence of different factors, as well as to rank intra and inter laboratory performance.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2454/42711
url https://hdl.handle.net/2454/42711
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv © 2021 The Authors. Creative Commons Attribution 4.0 International
https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv © 2021 The Authors. Creative Commons Attribution 4.0 International
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/zip
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
instname:Universidad Pública de Navarra
instname_str Universidad Pública de Navarra
reponame_str Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
collection Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
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