The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones

Proteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells synthesize a wide variety of molecular chaperones tha...

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Detalles Bibliográficos
Autores: Velasco Carneros, Lorea, Dublang Irazabal, Leire, Moro Pérez, Fernando, Muga Villate, Arturo
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/37532
Acceso en línea:http://hdl.handle.net/10810/37532
Access Level:acceso abierto
Palabra clave:chaperones
post-translational modification
phosphorylation
human disaggregase
Hsp40
Hsp70
Hsp110
cysteine string protein
molecular chaperones
J-domain
co-chaperones
yeast Hsp110
multisite phosphorylation
conformational dynamics
legionella-pneumophila
crystal-structure
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spelling The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its CochaperonesVelasco Carneros, LoreaDublang Irazabal, LeireMoro Pérez, FernandoMuga Villate, Arturochaperonespost-translational modificationphosphorylationhuman disaggregaseHsp40Hsp70Hsp110cysteine string proteinmolecular chaperonesJ-domainco-chaperonesyeast Hsp110multisite phosphorylationconformational dynamicslegionella-pneumophilacrystal-structureProteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells synthesize a wide variety of molecular chaperones that assist folding of other proteins and avoid their aggregation, which unfortunately is unavoidable under acute stress conditions. A protein machinery in metazoa, composed of representatives of the Hsp70, Hsp40, and Hsp110 chaperone families, can reactivate protein aggregates. We revised herein the phosphorylation sites found so far in members of these chaperone families and the functional consequences associated with some of them. We also discuss how phosphorylation might regulate the chaperone activity and the interaction of human Hsp70 with its accessory and client proteins. Finally, we present the information that would be necessary to decrypt the effect that post-translational modifications, and especially phosphorylation, could have on the biological activity of the Hsp70 system, known as the chaperone code.The Agencia Espanola de Investigacion/Fondos de Desarrollo Regional (AEI/FEDER, UE), [BFU2016-75983] and the Basque Government [IT1201-19] provided financial support for this work. L.V. and L.D. are supported by predoctoral grants from the University of the Basque Country and the Spanish Ministry of Economy, Industry and Competitiveness respectively.MDPI202020202019info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/37532reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoIngléshttps://www.mdpi.com/1422-0067/20/17/4122info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/3.0/es/This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Attribution 4.0 International (CC BY 4.0)Atribución 3.0 Españaoai:addi.ehu.eus:10810/375322026-06-18T09:23:17Z
dc.title.none.fl_str_mv The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
title The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
spellingShingle The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
Velasco Carneros, Lorea
chaperones
post-translational modification
phosphorylation
human disaggregase
Hsp40
Hsp70
Hsp110
cysteine string protein
molecular chaperones
J-domain
co-chaperones
yeast Hsp110
multisite phosphorylation
conformational dynamics
legionella-pneumophila
crystal-structure
title_short The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
title_full The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
title_fullStr The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
title_full_unstemmed The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
title_sort The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones
dc.creator.none.fl_str_mv Velasco Carneros, Lorea
Dublang Irazabal, Leire
Moro Pérez, Fernando
Muga Villate, Arturo
author Velasco Carneros, Lorea
author_facet Velasco Carneros, Lorea
Dublang Irazabal, Leire
Moro Pérez, Fernando
Muga Villate, Arturo
author_role author
author2 Dublang Irazabal, Leire
Moro Pérez, Fernando
Muga Villate, Arturo
author2_role author
author
author
dc.subject.none.fl_str_mv chaperones
post-translational modification
phosphorylation
human disaggregase
Hsp40
Hsp70
Hsp110
cysteine string protein
molecular chaperones
J-domain
co-chaperones
yeast Hsp110
multisite phosphorylation
conformational dynamics
legionella-pneumophila
crystal-structure
topic chaperones
post-translational modification
phosphorylation
human disaggregase
Hsp40
Hsp70
Hsp110
cysteine string protein
molecular chaperones
J-domain
co-chaperones
yeast Hsp110
multisite phosphorylation
conformational dynamics
legionella-pneumophila
crystal-structure
description Proteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells synthesize a wide variety of molecular chaperones that assist folding of other proteins and avoid their aggregation, which unfortunately is unavoidable under acute stress conditions. A protein machinery in metazoa, composed of representatives of the Hsp70, Hsp40, and Hsp110 chaperone families, can reactivate protein aggregates. We revised herein the phosphorylation sites found so far in members of these chaperone families and the functional consequences associated with some of them. We also discuss how phosphorylation might regulate the chaperone activity and the interaction of human Hsp70 with its accessory and client proteins. Finally, we present the information that would be necessary to decrypt the effect that post-translational modifications, and especially phosphorylation, could have on the biological activity of the Hsp70 system, known as the chaperone code.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/37532
url http://hdl.handle.net/10810/37532
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://www.mdpi.com/1422-0067/20/17/4122
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/3.0/es/
Atribución 3.0 España
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/3.0/es/
Atribución 3.0 España
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Addi. Archivo Digital para la Docencia y la Investigación
instname:Universidad del País Vasco
instname_str Universidad del País Vasco
reponame_str Addi. Archivo Digital para la Docencia y la Investigación
collection Addi. Archivo Digital para la Docencia y la Investigación
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.301603

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