Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress

11 p.-2 fig.-3 tab.

Detalles Bibliográficos
Autores: Griesser, Eva, Vemula, Venukumar, Mónico, Andreia, Pérez-Sala, Dolores, Fedorova, Maria
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/243043
Acceso en línea:http://hdl.handle.net/10261/243043
Access Level:acceso abierto
Palabra clave:Nitroxidative stress
Cardiac cells
Vimentin
Actin
Tubulin
Posttranslational modifications
Lipoxidation
Redox signaling
Cysteine
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spelling Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stressGriesser, EvaVemula, VenukumarMónico, AndreiaPérez-Sala, DoloresFedorova, MariaNitroxidative stressCardiac cellsVimentinActinTubulinPosttranslational modificationsLipoxidationRedox signalingCysteine11 p.-2 fig.-3 tab.The cytoskeleton is a supramolecular structure consisting of interacting protein networks that support cell dynamics in essential processes such as migration and division, as well as in responses to stress. Fast cytoskeletal remodeling is achieved with the participation of regulatory proteins and posttranslational modifications (PTMs).Redox-related PTMs are emerging as critical players in cytoskeletal regulation. Here we used a cellular model of mild nitroxidative stress in which a peroxynitrite donor induced transient changes in the organization of three key cytoskeletal proteins, i.e., vimentin, actin and tubulin. Nitroxidative stress-induced reconfiguration of intermediate filaments, microtubules and actin structures were further correlated with their PTM profiles and dynamics of the PTM landscape. Using high-resolution mass spectrometry, 62 different PTMs were identified and relatively quantified in vimentin, actin and tubulin, including 12 enzymatic, 13 oxidative and 2 nitric oxidederived modifications as well as 35 modifications by carbonylated lipid peroxidation products, thus evidencing the occurrence of a chain reaction with formation of numerous reactive species and activation of multiple signaling pathways. Our results unveil the presence of certain modifications under basal conditions and their modulation in response to stress in a target-, residue- and reactive species-dependent manner. Thus, some modifications accumulated during the experiment whereas others varied transiently. Moreover, we identified protein PTM “hot spots”, such as the single cysteine residue of vimentin, which was detected in seven modified forms, thus, supporting its role in PTM crosstalk and redox sensing. Finally, identification of novel PTMs in these proteins paves the way for unveiling new cytoskeleton regulatory mechanisms.This work was funded by Deutsche Forschungsgemeinschaft (DFG;FE-1236/31 to M.F.), European Regional Development Fund (ERDF,European Union and Free State Saxony; 100146238 and 100121468 to MF), and MASSTRPLAN project funded by the Marie Sklodowska-Curie EU Framework for Research and Innovation Horizon 2020 (Grant Agreement No. 675132, to MF and DPS). EG STSM at CIB-CSIC was supported by COST Action CM1001. DPS work has been supported by Agencia Estatal de Investigación, MINECO/ERDF (grants SAF2015-68590R and RTI2018-097624-B-I00), and ISCIII/ERDF (RETIC ARADYAL RD16/0006/0021).Peer reviewedElsevierGerman Research FoundationEuropean CommissionAgencia Estatal de Investigación (España)Ministerio de Economía y Competitividad (España)Instituto de Salud Carlos IIIMónico, Andreia [0000-0003-4855-8241]Pérez-Sala, Dolores [0000-0003-0600-665X]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202120212021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/243043reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/EC/H2020/675132info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2015-68590Rinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-097624-B-I00https://doi.org/10.1016/j.redox.2021.102014Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2430432026-05-22T06:33:51Z
dc.title.none.fl_str_mv Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
title Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
spellingShingle Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
Griesser, Eva
Nitroxidative stress
Cardiac cells
Vimentin
Actin
Tubulin
Posttranslational modifications
Lipoxidation
Redox signaling
Cysteine
title_short Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
title_full Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
title_fullStr Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
title_full_unstemmed Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
title_sort Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress
dc.creator.none.fl_str_mv Griesser, Eva
Vemula, Venukumar
Mónico, Andreia
Pérez-Sala, Dolores
Fedorova, Maria
author Griesser, Eva
author_facet Griesser, Eva
Vemula, Venukumar
Mónico, Andreia
Pérez-Sala, Dolores
Fedorova, Maria
author_role author
author2 Vemula, Venukumar
Mónico, Andreia
Pérez-Sala, Dolores
Fedorova, Maria
author2_role author
author
author
author
dc.contributor.none.fl_str_mv German Research Foundation
European Commission
Agencia Estatal de Investigación (España)
Ministerio de Economía y Competitividad (España)
Instituto de Salud Carlos III
Mónico, Andreia [0000-0003-4855-8241]
Pérez-Sala, Dolores [0000-0003-0600-665X]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Nitroxidative stress
Cardiac cells
Vimentin
Actin
Tubulin
Posttranslational modifications
Lipoxidation
Redox signaling
Cysteine
topic Nitroxidative stress
Cardiac cells
Vimentin
Actin
Tubulin
Posttranslational modifications
Lipoxidation
Redox signaling
Cysteine
description 11 p.-2 fig.-3 tab.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021
2021
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/10261/243043
url http://hdl.handle.net/10261/243043
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/EC/H2020/675132
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2015-68590R
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-097624-B-I00
https://doi.org/10.1016/j.redox.2021.102014
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 15.811543

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