Altered intracellular calcium homeostasis and endoplasmic reticulum redox state in Saccharomyces cerevisiae cells lacking Grx6 glutaredoxin.
Identifieur interne : 000574 ( Main/Exploration ); précédent : 000573; suivant : 000575Altered intracellular calcium homeostasis and endoplasmic reticulum redox state in Saccharomyces cerevisiae cells lacking Grx6 glutaredoxin.
Auteurs : Judit Puigpin S [Espagne] ; Celia Casas [Espagne] ; Enrique Herrero [Autriche]Source :
- Molecular biology of the cell [ 1939-4586 ] ; 2015.
Descripteurs français
- KwdFr :
- Appareil de Golgi (métabolisme), Calcium (métabolisme), Cycle cellulaire (MeSH), Cytoplasme (métabolisme), Cytosol (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Homéostasie (MeSH), Oxydoréduction (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Réticulum endoplasmique (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Thiols (métabolisme), Transport des ions (MeSH), Transport des protéines (MeSH).
- MESH :
- génétique : Glutarédoxines, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Appareil de Golgi, Calcium, Cytoplasme, Cytosol, Glutarédoxines, Protéines de Saccharomyces cerevisiae, Réticulum endoplasmique, Saccharomyces cerevisiae, Thiols.
- Cycle cellulaire, Homéostasie, Oxydoréduction, Transport des ions, Transport des protéines.
English descriptors
- KwdEn :
- Calcium (metabolism), Cell Cycle (MeSH), Cytoplasm (metabolism), Cytosol (metabolism), Endoplasmic Reticulum (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Golgi Apparatus (metabolism), Homeostasis (MeSH), Ion Transport (MeSH), Oxidation-Reduction (MeSH), Protein Transport (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sulfhydryl Compounds (metabolism).
- MESH :
- chemical , genetics : Glutaredoxins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Calcium, Glutaredoxins, Saccharomyces cerevisiae Proteins, Sulfhydryl Compounds.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cytoplasm, Cytosol, Endoplasmic Reticulum, Golgi Apparatus, Saccharomyces cerevisiae.
- Cell Cycle, Homeostasis, Ion Transport, Oxidation-Reduction, Protein Transport.
Abstract
Glutaredoxin 6 (Grx6) of Saccharomyces cerevisiae is an integral thiol oxidoreductase protein of the endoplasmic reticulum/Golgi vesicles. Its absence alters the redox equilibrium of the reticulum lumen toward a more oxidized state, thus compensating the defects in protein folding/secretion and cell growth caused by low levels of the oxidase Ero1. In addition, null mutants in GRX6 display a more intense unfolded protein response than wild-type cells upon treatment with inducers of this pathway. These observations support a role of Grx6 in regulating the glutathionylation of thiols of endoplasmic reticulum/Golgi target proteins and consequently the equilibrium between reduced and oxidized glutathione in the lumen of these compartments. A specific function influenced by Grx6 activity is the homeostasis of intracellular calcium. Grx6-deficient mutants have reduced levels of calcium in the ER lumen, whereas accumulation occurs at the cytosol from extracellular sources. This results in permanent activation of the calcineurin-dependent pathway in these cells. Some but not all the phenotypes of the mutant are coincident with those of mutants deficient in intracellular calcium transporters, such as the Golgi Pmr1 protein. The results presented in this study provide evidence for redox regulation of calcium homeostasis in yeast cells.
DOI: 10.1091/mbc.E14-06-1137
PubMed: 25355945
PubMed Central: PMC4279222
Affiliations:
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Le document en format XML
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(metabolism)</term><term>Homeostasis (MeSH)</term><term>Ion Transport (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Transport (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Appareil de Golgi (métabolisme)</term><term>Calcium (métabolisme)</term><term>Cycle cellulaire (MeSH)</term><term>Cytoplasme (métabolisme)</term><term>Cytosol (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Réticulum endoplasmique (métabolisme)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Thiols (métabolisme)</term><term>Transport des ions (MeSH)</term><term>Transport des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Glutaredoxins</term><term>Saccharomyces cerevisiae Proteins</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term><term>Cytosol</term><term>Endoplasmic Reticulum</term><term>Golgi Apparatus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Calcium</term><term>Cytoplasme</term><term>Cytosol</term><term>Glutarédoxines</term><term>Protéines de Saccharomyces cerevisiae</term><term>Réticulum endoplasmique</term><term>Saccharomyces cerevisiae</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Cycle</term><term>Homeostasis</term><term>Ion Transport</term><term>Oxidation-Reduction</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cycle cellulaire</term><term>Homéostasie</term><term>Oxydoréduction</term><term>Transport des ions</term><term>Transport des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin 6 (Grx6) of Saccharomyces cerevisiae is an integral thiol oxidoreductase protein of the endoplasmic reticulum/Golgi vesicles. Its absence alters the redox equilibrium of the reticulum lumen toward a more oxidized state, thus compensating the defects in protein folding/secretion and cell growth caused by low levels of the oxidase Ero1. In addition, null mutants in GRX6 display a more intense unfolded protein response than wild-type cells upon treatment with inducers of this pathway. These observations support a role of Grx6 in regulating the glutathionylation of thiols of endoplasmic reticulum/Golgi target proteins and consequently the equilibrium between reduced and oxidized glutathione in the lumen of these compartments. A specific function influenced by Grx6 activity is the homeostasis of intracellular calcium. Grx6-deficient mutants have reduced levels of calcium in the ER lumen, whereas accumulation occurs at the cytosol from extracellular sources. This results in permanent activation of the calcineurin-dependent pathway in these cells. Some but not all the phenotypes of the mutant are coincident with those of mutants deficient in intracellular calcium transporters, such as the Golgi Pmr1 protein. The results presented in this study provide evidence for redox regulation of calcium homeostasis in yeast cells. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25355945</PMID><DateCompleted><Year>2015</Year><Month>08</Month><Day>17</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>1</Issue><PubDate><Year>2015</Year><Month>Jan</Month><Day>01</Day></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Altered intracellular calcium homeostasis and endoplasmic reticulum redox state in Saccharomyces cerevisiae cells lacking Grx6 glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>104-16</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E14-06-1137</ELocationID><Abstract><AbstractText>Glutaredoxin 6 (Grx6) of Saccharomyces cerevisiae is an integral thiol oxidoreductase protein of the endoplasmic reticulum/Golgi vesicles. Its absence alters the redox equilibrium of the reticulum lumen toward a more oxidized state, thus compensating the defects in protein folding/secretion and cell growth caused by low levels of the oxidase Ero1. In addition, null mutants in GRX6 display a more intense unfolded protein response than wild-type cells upon treatment with inducers of this pathway. These observations support a role of Grx6 in regulating the glutathionylation of thiols of endoplasmic reticulum/Golgi target proteins and consequently the equilibrium between reduced and oxidized glutathione in the lumen of these compartments. A specific function influenced by Grx6 activity is the homeostasis of intracellular calcium. Grx6-deficient mutants have reduced levels of calcium in the ER lumen, whereas accumulation occurs at the cytosol from extracellular sources. This results in permanent activation of the calcineurin-dependent pathway in these cells. Some but not all the phenotypes of the mutant are coincident with those of mutants deficient in intracellular calcium transporters, such as the Golgi Pmr1 protein. The results presented in this study provide evidence for redox regulation of calcium homeostasis in yeast cells. </AbstractText><CopyrightInformation>© 2015 Puigpinós et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Puigpinós</LastName><ForeName>Judit</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, IRBLleida, 25198 Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Casas</LastName><ForeName>Celia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, IRBLleida, 25198 Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, IRBLleida, 25198 Lleida, Spain enric.herrero@cmb.udl.cat.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Biol Cell</MedlineTA><NlmUniqueID>9201390</NlmUniqueID><ISSNLinking>1059-1524</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C527470">Grx6 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae 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MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006056" MajorTopicYN="N">Golgi Apparatus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017136" MajorTopicYN="N">Ion Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein 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IdType="pubmed">16607396</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Autriche</li><li>Espagne</li></country><region><li>Catalogne</li></region></list><tree><country name="Espagne"><region name="Catalogne"><name sortKey="Puigpin S, Judit" sort="Puigpin S, Judit" uniqKey="Puigpin S J" first="Judit" last="Puigpin S">Judit Puigpin S</name></region><name sortKey="Casas, Celia" sort="Casas, Celia" uniqKey="Casas C" first="Celia" last="Casas">Celia Casas</name></country><country name="Autriche"><noRegion><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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