The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation

The AMPK/Snf1 kinase has a central role in carbon metabolism homeostasis in Saccharomyces cerevisiae. In this study, we show that Snf1 activity, which requires phosphorylation of the Thr210 residue, is needed for protection against selenite toxicity. Such protection involves the Elm1 kinase, which a...

ver descrição completa

Detalhes bibliográficos
Autores: Pérez Sampietro, María, Casas Herranz, Celia, Herrero Perpiñán, Enrique
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2013
País:España
Recursos:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositório:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10459.1/47224
Acesso em linha:https://doi.org/10.1371/journal.pone.0058283
http://hdl.handle.net/10459.1/47224
Access Level:Acceso aberto
Palavra-chave:Llevat de cervesa
Saccharomyces cerevisiae
Biologia molecular
Bioquímica
id ES_d74f3d9404c18e7e3bbdc016818c2f0b
oai_identifier_str oai:recercat.cat:10459.1/47224
network_acronym_str ES
network_name_str España
repository_id_str
spelling The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidationPérez Sampietro, MaríaCasas Herranz, CeliaHerrero Perpiñán, EnriqueLlevat de cervesaSaccharomyces cerevisiaeBiologia molecularBioquímicaThe AMPK/Snf1 kinase has a central role in carbon metabolism homeostasis in Saccharomyces cerevisiae. In this study, we show that Snf1 activity, which requires phosphorylation of the Thr210 residue, is needed for protection against selenite toxicity. Such protection involves the Elm1 kinase, which acts upstream of Snf1 to activate it. Basal Snf1 activity is sufficient for the defense against selenite, although Snf1 Thr210 phosphorylation levels become increased at advanced treatment times, probably by inhibition of the Snf1 dephosphorylation function of the Reg1 phosphatase. Contrary to glucose deprivation, Snf1 remains cytosolic during selenite treatment, and the protective function of the kinase does not require its known nuclear effectors. Upon selenite treatment, a null snf1 mutant displays higher levels of oxidized versus reduced glutathione compared to wild type cells, and its hypersensitivity to the agent is rescued by overexpression of the glutathione reductase gene GLR1. In the presence of agents such as diethyl maleate or diamide, which cause alterations in glutathione redox homeostasis by increasing the levels of oxidized glutathione, yeast cells also require Snf1 in an Elm1-dependent manner for growth. These observations demonstrate a role of Snf1 to protect yeast cells in situations where glutathione-dependent redox homeostasis is altered to a more oxidant intracellular environment and associates AMPK to responses against oxidative stress.This work was funded by Ministerio de Economía y Competitividad (Spain) (grants BFU2010-17656 and CSD2007-0020) and Generalitat de Catalunya (grant 2009/SGR/196). MPS is the recipient of a predoctoral fellowship from Generalitat de Catalunya. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Public Library of Science2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://doi.org/10.1371/journal.pone.0058283http://hdl.handle.net/10459.1/47224reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)Inglésinfo:eu-repo/grantAgreement/MICINN//BFU2010-17656info:eu-repo/grantAgreement/MEC//CSD2007-0020Reproducció del document publicat a https://doi.org/10.1371/journal.pone.0058283PLoS ONE, 2013, vol. 8, núm. 3, e58283cc-by (c) Pérez-Sampietro et al., 2013info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/3.0/es/oai:recercat.cat:10459.1/472242026-05-29T05:05:01Z
dc.title.none.fl_str_mv The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
title The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
spellingShingle The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
Pérez Sampietro, María
Llevat de cervesa
Saccharomyces cerevisiae
Biologia molecular
Bioquímica
title_short The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
title_full The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
title_fullStr The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
title_full_unstemmed The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
title_sort The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutatione oxidation
dc.creator.none.fl_str_mv Pérez Sampietro, María
Casas Herranz, Celia
Herrero Perpiñán, Enrique
author Pérez Sampietro, María
author_facet Pérez Sampietro, María
Casas Herranz, Celia
Herrero Perpiñán, Enrique
author_role author
author2 Casas Herranz, Celia
Herrero Perpiñán, Enrique
author2_role author
author
dc.subject.none.fl_str_mv Llevat de cervesa
Saccharomyces cerevisiae
Biologia molecular
Bioquímica
topic Llevat de cervesa
Saccharomyces cerevisiae
Biologia molecular
Bioquímica
description The AMPK/Snf1 kinase has a central role in carbon metabolism homeostasis in Saccharomyces cerevisiae. In this study, we show that Snf1 activity, which requires phosphorylation of the Thr210 residue, is needed for protection against selenite toxicity. Such protection involves the Elm1 kinase, which acts upstream of Snf1 to activate it. Basal Snf1 activity is sufficient for the defense against selenite, although Snf1 Thr210 phosphorylation levels become increased at advanced treatment times, probably by inhibition of the Snf1 dephosphorylation function of the Reg1 phosphatase. Contrary to glucose deprivation, Snf1 remains cytosolic during selenite treatment, and the protective function of the kinase does not require its known nuclear effectors. Upon selenite treatment, a null snf1 mutant displays higher levels of oxidized versus reduced glutathione compared to wild type cells, and its hypersensitivity to the agent is rescued by overexpression of the glutathione reductase gene GLR1. In the presence of agents such as diethyl maleate or diamide, which cause alterations in glutathione redox homeostasis by increasing the levels of oxidized glutathione, yeast cells also require Snf1 in an Elm1-dependent manner for growth. These observations demonstrate a role of Snf1 to protect yeast cells in situations where glutathione-dependent redox homeostasis is altered to a more oxidant intracellular environment and associates AMPK to responses against oxidative stress.
publishDate 2013
dc.date.none.fl_str_mv 2013
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://doi.org/10.1371/journal.pone.0058283
http://hdl.handle.net/10459.1/47224
url https://doi.org/10.1371/journal.pone.0058283
http://hdl.handle.net/10459.1/47224
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/MICINN//BFU2010-17656
info:eu-repo/grantAgreement/MEC//CSD2007-0020
Reproducció del document publicat a https://doi.org/10.1371/journal.pone.0058283
PLoS ONE, 2013, vol. 8, núm. 3, e58283
dc.rights.none.fl_str_mv cc-by (c) Pérez-Sampietro et al., 2013
info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/3.0/es/
rights_invalid_str_mv cc-by (c) Pérez-Sampietro et al., 2013
http://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv 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_ 1869420990780407809
score 15.812455

Registros relacionados