Physical interaction between the MAPK Slt2 of the PKC1-MAPK pathway and Grx3/Grx4 glutaredoxins is required for the oxidative stress response in budding yeast.
Identifieur interne : 000329 ( Main/Exploration ); précédent : 000328; suivant : 000330Physical interaction between the MAPK Slt2 of the PKC1-MAPK pathway and Grx3/Grx4 glutaredoxins is required for the oxidative stress response in budding yeast.
Auteurs : Nuria Pujol-Carrion [Espagne] ; Maria Angeles De La Torre-Ruiz [Espagne]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2017.
Descripteurs français
- KwdFr :
- Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Maturation post-traductionnelle des protéines (MeSH), Mitogen-Activated Protein Kinases (composition chimique), Mitogen-Activated Protein Kinases (métabolisme), Motifs et domaines d'intéraction protéique (MeSH), Multimérisation de protéines (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Phosphorylation (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (enzymologie), Stress oxydatif (MeSH), Système de signalisation des MAP kinases (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Mitogen-Activated Protein Kinases, Oxidoreductases, Protéines de Saccharomyces cerevisiae.
- enzymologie : Saccharomyces cerevisiae.
- métabolisme : Glutarédoxines, Mitogen-Activated Protein Kinases, Oxidoreductases, Protéines de Saccharomyces cerevisiae.
- Maturation post-traductionnelle des protéines, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Oxydoréduction, Phosphorylation, Stress oxydatif, Système de signalisation des MAP kinases, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Glutaredoxins (chemistry), Glutaredoxins (metabolism), MAP Kinase Signaling System (MeSH), Mitogen-Activated Protein Kinases (chemistry), Mitogen-Activated Protein Kinases (metabolism), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Phosphorylation (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Multimerization (MeSH), Protein Processing, Post-Translational (MeSH), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Mitogen-Activated Protein Kinases, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutaredoxins, Mitogen-Activated Protein Kinases, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- enzymology : Saccharomyces cerevisiae.
- Amino Acid Sequence, MAP Kinase Signaling System, Oxidation-Reduction, Oxidative Stress, Phosphorylation, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Processing, Post-Translational.
Abstract
This study demonstrates that both monothiol glutaredoxins Grx3 and Grx4 physically interact with the MAPK Slt2 forming a complex involved in the cellular response to oxidative stress. The simultaneous absence of Grx3 and Grx4 provokes a serious impairment in cell viability, Slt2 activation and Rlm1 transcription in response to oxidative stress. Both in vivo and in vitro results clearly show that Slt2 can independently bind either Grx3 or Grx4 proteins. Our results suggest that Slt2 form iron/sulphur bridged clusters with Grx3 and Grx4. For the assembly of this complex, cysteines of the active site of each Grx3/4 glutaredoxins, glutathione and specific cysteine residues from Slt2 provide the ligands. One of the ligands of Slt2 is required for its dimerisation upon oxidative treatment and iron repletion. These interactions are relevant for the oxidative response, given that mutants in the cysteine ligands identified in the complex show a severe impairment of both cell viability and Slt2 phosphorylation upon oxidative stress. Grx4 is the relevant glutaredoxin that regulates Slt2 phosphorylation under oxidative conditions precluding cell survival. Our studies contribute to extend the functions of both monothiol glutaredoxins to the regulation of a MAPK in the context of the oxidative stress response.
DOI: 10.1016/j.freeradbiomed.2016.12.023
PubMed: 28007574
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (metabolism)</term>
<term>MAP Kinase Signaling System (MeSH)</term>
<term>Mitogen-Activated Protein Kinases (chemistry)</term>
<term>Mitogen-Activated Protein Kinases (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidative Stress (MeSH)</term>
<term>Oxidoreductases (chemistry)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Interaction Domains and Motifs (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Mitogen-Activated Protein Kinases (composition chimique)</term>
<term>Mitogen-Activated Protein Kinases (métabolisme)</term>
<term>Motifs et domaines d'intéraction protéique (MeSH)</term>
<term>Multimérisation de protéines (MeSH)</term>
<term>Oxidoreductases (composition chimique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Stress oxydatif (MeSH)</term>
<term>Système de signalisation des MAP kinases (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>Oxidoreductases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>Oxidoreductases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>Oxidoreductases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<term>Mitogen-Activated Protein Kinases</term>
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<term>Protéines de Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>MAP Kinase Signaling System</term>
<term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
<term>Phosphorylation</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Multimerization</term>
<term>Protein Processing, Post-Translational</term>
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<term>Motifs et domaines d'intéraction protéique</term>
<term>Multimérisation de protéines</term>
<term>Oxydoréduction</term>
<term>Phosphorylation</term>
<term>Stress oxydatif</term>
<term>Système de signalisation des MAP kinases</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">This study demonstrates that both monothiol glutaredoxins Grx3 and Grx4 physically interact with the MAPK Slt2 forming a complex involved in the cellular response to oxidative stress. The simultaneous absence of Grx3 and Grx4 provokes a serious impairment in cell viability, Slt2 activation and Rlm1 transcription in response to oxidative stress. Both in vivo and in vitro results clearly show that Slt2 can independently bind either Grx3 or Grx4 proteins. Our results suggest that Slt2 form iron/sulphur bridged clusters with Grx3 and Grx4. For the assembly of this complex, cysteines of the active site of each Grx3/4 glutaredoxins, glutathione and specific cysteine residues from Slt2 provide the ligands. One of the ligands of Slt2 is required for its dimerisation upon oxidative treatment and iron repletion. These interactions are relevant for the oxidative response, given that mutants in the cysteine ligands identified in the complex show a severe impairment of both cell viability and Slt2 phosphorylation upon oxidative stress. Grx4 is the relevant glutaredoxin that regulates Slt2 phosphorylation under oxidative conditions precluding cell survival. Our studies contribute to extend the functions of both monothiol glutaredoxins to the regulation of a MAPK in the context of the oxidative stress response.</div>
</front>
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<ArticleTitle>Physical interaction between the MAPK Slt2 of the PKC1-MAPK pathway and Grx3/Grx4 glutaredoxins is required for the oxidative stress response in budding yeast.</ArticleTitle>
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<Abstract><AbstractText>This study demonstrates that both monothiol glutaredoxins Grx3 and Grx4 physically interact with the MAPK Slt2 forming a complex involved in the cellular response to oxidative stress. The simultaneous absence of Grx3 and Grx4 provokes a serious impairment in cell viability, Slt2 activation and Rlm1 transcription in response to oxidative stress. Both in vivo and in vitro results clearly show that Slt2 can independently bind either Grx3 or Grx4 proteins. Our results suggest that Slt2 form iron/sulphur bridged clusters with Grx3 and Grx4. For the assembly of this complex, cysteines of the active site of each Grx3/4 glutaredoxins, glutathione and specific cysteine residues from Slt2 provide the ligands. One of the ligands of Slt2 is required for its dimerisation upon oxidative treatment and iron repletion. These interactions are relevant for the oxidative response, given that mutants in the cysteine ligands identified in the complex show a severe impairment of both cell viability and Slt2 phosphorylation upon oxidative stress. Grx4 is the relevant glutaredoxin that regulates Slt2 phosphorylation under oxidative conditions precluding cell survival. Our studies contribute to extend the functions of both monothiol glutaredoxins to the regulation of a MAPK in the context of the oxidative stress response.</AbstractText>
<CopyrightInformation>Copyright © 2016 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pujol-Carrion</LastName>
<ForeName>Nuria</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Basic Medical Sciences, IRB-Lleida. University of Lleida, Av. Alcalde Rovira Roure no 80, 25198 Lleida, Spain.</Affiliation>
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<Author ValidYN="Y"><LastName>Torre-Ruiz</LastName>
<ForeName>Maria Angeles de la</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Department of Basic Medical Sciences, IRB-Lleida. University of Lleida, Av. Alcalde Rovira Roure no 80, 25198 Lleida, Spain. Electronic address: madelatorre@cmb.udl.cat.</Affiliation>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<NameOfSubstance UI="C516012">Grx4 protein, S cerevisiae</NameOfSubstance>
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<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
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<Keyword MajorTopicYN="Y">Cell survival</Keyword>
<Keyword MajorTopicYN="Y">Glutaredoxins</Keyword>
<Keyword MajorTopicYN="Y">Iron</Keyword>
<Keyword MajorTopicYN="Y">MAPK</Keyword>
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