Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau

The neocortex of P301S mice, used as a model of fronto-temporal lobar degeneration linked to tau mutation (FTLD-tau), and wild-type mice, both aged 9 months, were analyzed with conventional label-free phosphoproteomics and SWATH-MS (sequential window acquisition of all theoretical fragment ion spect...

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Autores: Ferrer, Isidro (Ferrer Abizanda), Andrés Benito, Pol, Ausín, Karina, Cartas Cejudo, Paz, Lachén Montes, Mercedes, Río Fernández, José Antonio del, Fernández Irigoyen, Joaquín, Santamaría, Enrique
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2022
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/196240
Acceso en línea:https://hdl.handle.net/2445/196240
Access Level:acceso abierto
Palabra clave:Proteòmica
Citosquelet
Proteïnes quinases
Proteomics
Cytoskeleton
Protein kinases
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spelling Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-TauFerrer, Isidro (Ferrer Abizanda)Andrés Benito, PolAusín, KarinaCartas Cejudo, PazLachén Montes, MercedesRío Fernández, José Antonio delFernández Irigoyen, JoaquínSantamaría, EnriqueProteòmicaCitosqueletProteïnes quinasesProteomicsCytoskeletonProtein kinasesThe neocortex of P301S mice, used as a model of fronto-temporal lobar degeneration linked to tau mutation (FTLD-tau), and wild-type mice, both aged 9 months, were analyzed with conventional label-free phosphoproteomics and SWATH-MS (sequential window acquisition of all theoretical fragment ion spectra mass spectrometry) to assess the (phospho)proteomes. The total number of identified dysregulated phosphoproteins was 328 corresponding to 524 phosphorylation sites. The majority of dysregulated phosphoproteins, most of them hyperphosphorylated, were proteins of the membranes, synapses, membrane trafficking, membrane vesicles linked to endo- and exocytosis, cytoplasmic vesicles, and cytoskeleton. Another group was composed of kinases. In contrast, proteins linked to DNA, RNA metabolism, RNA splicing, and protein synthesis were hypophosphorylated. Other pathways modulating energy metabolism, cell signaling, Golgi apparatus, carbohydrates, and lipids are also targets of dysregulated protein phosphorylation in P301S mice. The present results, together with accompanying immunohistochemical and Western-blotting studies, show widespread abnormal phosphorylation of proteins, in addition to protein tau, in P301S mice. These observations point to dysregulated protein phosphorylation as a relevant contributory pathogenic component of tauopathies.Lippincott, Williams & Wilkins. Wolters Kluwer Health2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://hdl.handle.net/2445/196240Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésVersió postprint del document publicat a: https://doi.org/10.1093/jnen/nlac062Journal of Neuropathology and Experimental Neurology, 2022, vol. 81, num. 9, p. 696-706https://doi.org/10.1093/jnen/nlac062(c) American Association of Neuropathologists, 2022info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1962402026-05-27T06:46:51Z
dc.title.none.fl_str_mv Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
title Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
spellingShingle Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
Ferrer, Isidro (Ferrer Abizanda)
Proteòmica
Citosquelet
Proteïnes quinases
Proteomics
Cytoskeleton
Protein kinases
title_short Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
title_full Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
title_fullStr Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
title_full_unstemmed Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
title_sort Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau
dc.creator.none.fl_str_mv Ferrer, Isidro (Ferrer Abizanda)
Andrés Benito, Pol
Ausín, Karina
Cartas Cejudo, Paz
Lachén Montes, Mercedes
Río Fernández, José Antonio del
Fernández Irigoyen, Joaquín
Santamaría, Enrique
author Ferrer, Isidro (Ferrer Abizanda)
author_facet Ferrer, Isidro (Ferrer Abizanda)
Andrés Benito, Pol
Ausín, Karina
Cartas Cejudo, Paz
Lachén Montes, Mercedes
Río Fernández, José Antonio del
Fernández Irigoyen, Joaquín
Santamaría, Enrique
author_role author
author2 Andrés Benito, Pol
Ausín, Karina
Cartas Cejudo, Paz
Lachén Montes, Mercedes
Río Fernández, José Antonio del
Fernández Irigoyen, Joaquín
Santamaría, Enrique
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Proteòmica
Citosquelet
Proteïnes quinases
Proteomics
Cytoskeleton
Protein kinases
topic Proteòmica
Citosquelet
Proteïnes quinases
Proteomics
Cytoskeleton
Protein kinases
description The neocortex of P301S mice, used as a model of fronto-temporal lobar degeneration linked to tau mutation (FTLD-tau), and wild-type mice, both aged 9 months, were analyzed with conventional label-free phosphoproteomics and SWATH-MS (sequential window acquisition of all theoretical fragment ion spectra mass spectrometry) to assess the (phospho)proteomes. The total number of identified dysregulated phosphoproteins was 328 corresponding to 524 phosphorylation sites. The majority of dysregulated phosphoproteins, most of them hyperphosphorylated, were proteins of the membranes, synapses, membrane trafficking, membrane vesicles linked to endo- and exocytosis, cytoplasmic vesicles, and cytoskeleton. Another group was composed of kinases. In contrast, proteins linked to DNA, RNA metabolism, RNA splicing, and protein synthesis were hypophosphorylated. Other pathways modulating energy metabolism, cell signaling, Golgi apparatus, carbohydrates, and lipids are also targets of dysregulated protein phosphorylation in P301S mice. The present results, together with accompanying immunohistochemical and Western-blotting studies, show widespread abnormal phosphorylation of proteins, in addition to protein tau, in P301S mice. These observations point to dysregulated protein phosphorylation as a relevant contributory pathogenic component of tauopathies.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/196240
url https://hdl.handle.net/2445/196240
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1093/jnen/nlac062
Journal of Neuropathology and Experimental Neurology, 2022, vol. 81, num. 9, p. 696-706
https://doi.org/10.1093/jnen/nlac062
dc.rights.none.fl_str_mv (c) American Association of Neuropathologists, 2022
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) American Association of Neuropathologists, 2022
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Lippincott, Williams & Wilkins. Wolters Kluwer Health
publisher.none.fl_str_mv Lippincott, Williams & Wilkins. Wolters Kluwer Health
dc.source.none.fl_str_mv Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301629

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