Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics

p38α (encoded by MAPK14) is a protein kinase that regulates cellular responses to almost all types of environmental and intracellular stresses. Upon activation, p38α phosphorylates many substrates both in the cytoplasm and nucleus, allowing this pathway to regulate a wide variety of cellular process...

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Autores: Dan, Yuzhen, Radic, Nevenka, Gay i Marín, Marina, Fernández Torras, Adrià, Arauz, Gianluca, Vilaseca Casas, Marta, Aloy, Patrick, Canovas, Begoña, Nebreda, Àngel R.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/201174
Acceso en línea:https://hdl.handle.net/2445/201174
Access Level:acceso abierto
Palabra clave:Fosforilació
Proteòmica
Phosphorylation
Proteomics
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spelling Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomicsDan, YuzhenRadic, NevenkaGay i Marín, MarinaFernández Torras, AdriàArauz, GianlucaVilaseca Casas, MartaAloy, PatrickCanovas, BegoñaNebreda, Àngel R.FosforilacióProteòmicaPhosphorylationProteomicsp38α (encoded by MAPK14) is a protein kinase that regulates cellular responses to almost all types of environmental and intracellular stresses. Upon activation, p38α phosphorylates many substrates both in the cytoplasm and nucleus, allowing this pathway to regulate a wide variety of cellular processes. While the role of p38α in the stress response has been widely investigated, its implication in cell homeostasis is less understood. To investigate the signaling networks regulated by p38α in proliferating cancer cells, we performed quantitative proteomic and phosphoproteomic analyses in breast cancer cells in which this pathway had been either genetically targeted or chemically inhibited. Our study identified with high confidence 35 proteins and 82 phosphoproteins (114 phosphosites) that are modulated by p38α, and highlighted the implication of various protein kinases, including MK2 and mTOR, in the p38α-regulated signaling networks. Moreover, functional analyses revealed an important contribution of p38α to the regulation of cell adhesion, DNA replication and RNA metabolism. Indeed, we provide experimental evidence supporting that p38α facilitates cancer cell adhesion, and showed that this p38α function is likely mediated by the modulation of the adaptor protein ArgBP2. Collectively, our results illustrate the complexity of the p38α regulated signaling networks, provide valuable information on p38α-dependent phosphorylation events in cancer cells, and document a mechanism by which p38α can regulate cell adhesion.Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.Elsevier2023202320232023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion18 p.application/pdfhttps://hdl.handle.net/2445/201174Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona))reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.1016/j.mcpro.2023.100527Molecular & Cellular Proteomics, 2023, vol. 22, num. 4https://doi.org/10.1016/j.mcpro.2023.100527cc by-nc-nd (c) Dan, Yuzhen et al, 2023http://creativecommons.org/licenses/by-nc-nd/3.0/es/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/2011742026-05-29T05:05:01Z
dc.title.none.fl_str_mv Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
title Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
spellingShingle Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
Dan, Yuzhen
Fosforilació
Proteòmica
Phosphorylation
Proteomics
title_short Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
title_full Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
title_fullStr Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
title_full_unstemmed Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
title_sort Characterization of p38α signaling networks in cancer cells using quantitative proteomics and phosphoproteomics
dc.creator.none.fl_str_mv Dan, Yuzhen
Radic, Nevenka
Gay i Marín, Marina
Fernández Torras, Adrià
Arauz, Gianluca
Vilaseca Casas, Marta
Aloy, Patrick
Canovas, Begoña
Nebreda, Àngel R.
author Dan, Yuzhen
author_facet Dan, Yuzhen
Radic, Nevenka
Gay i Marín, Marina
Fernández Torras, Adrià
Arauz, Gianluca
Vilaseca Casas, Marta
Aloy, Patrick
Canovas, Begoña
Nebreda, Àngel R.
author_role author
author2 Radic, Nevenka
Gay i Marín, Marina
Fernández Torras, Adrià
Arauz, Gianluca
Vilaseca Casas, Marta
Aloy, Patrick
Canovas, Begoña
Nebreda, Àngel R.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Fosforilació
Proteòmica
Phosphorylation
Proteomics
topic Fosforilació
Proteòmica
Phosphorylation
Proteomics
description p38α (encoded by MAPK14) is a protein kinase that regulates cellular responses to almost all types of environmental and intracellular stresses. Upon activation, p38α phosphorylates many substrates both in the cytoplasm and nucleus, allowing this pathway to regulate a wide variety of cellular processes. While the role of p38α in the stress response has been widely investigated, its implication in cell homeostasis is less understood. To investigate the signaling networks regulated by p38α in proliferating cancer cells, we performed quantitative proteomic and phosphoproteomic analyses in breast cancer cells in which this pathway had been either genetically targeted or chemically inhibited. Our study identified with high confidence 35 proteins and 82 phosphoproteins (114 phosphosites) that are modulated by p38α, and highlighted the implication of various protein kinases, including MK2 and mTOR, in the p38α-regulated signaling networks. Moreover, functional analyses revealed an important contribution of p38α to the regulation of cell adhesion, DNA replication and RNA metabolism. Indeed, we provide experimental evidence supporting that p38α facilitates cancer cell adhesion, and showed that this p38α function is likely mediated by the modulation of the adaptor protein ArgBP2. Collectively, our results illustrate the complexity of the p38α regulated signaling networks, provide valuable information on p38α-dependent phosphorylation events in cancer cells, and document a mechanism by which p38α can regulate cell adhesion.Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
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/2445/201174
url https://hdl.handle.net/2445/201174
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1016/j.mcpro.2023.100527
Molecular & Cellular Proteomics, 2023, vol. 22, num. 4
https://doi.org/10.1016/j.mcpro.2023.100527
dc.rights.none.fl_str_mv cc by-nc-nd (c) Dan, Yuzhen et al, 2023
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by-nc-nd (c) Dan, Yuzhen et al, 2023
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 18 p.
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona))
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869407687836434432
score 15,81155

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