Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster.
Identifieur interne : 000A44 ( Main/Exploration ); précédent : 000A43; suivant : 000A45Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster.
Auteurs : Ulrich Mühlenhoff [Allemagne] ; Sabine Molik [Allemagne] ; José R. Godoy [Allemagne] ; Marta A. Uzarska [Allemagne] ; Nadine Richter [Allemagne] ; Andreas Seubert [Allemagne] ; Yan Zhang [États-Unis] ; Joanne Stubbe [États-Unis] ; Fabien Pierrel [France] ; Enrique Herrero [Espagne] ; Christopher Horst Lillig [Allemagne] ; Roland Lill [Allemagne]Source :
- Cell metabolism [ 1932-7420 ] ; 2010.
Descripteurs français
- KwdFr :
- Cytosol (métabolisme), Fer (métabolisme), Ferrosulfoprotéines (MeSH), Glutarédoxines (métabolisme), Levures (métabolisme), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Protéines (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Soufre (métabolisme), Transport biologique (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutaredoxins, Iron, Oxidoreductases, Proteins, Saccharomyces cerevisiae Proteins, Sulfur.
- metabolism : Cytosol, Yeasts.
- Biological Transport, Iron-Sulfur Proteins, Oxidation-Reduction.
Abstract
Iron is an essential nutrient for cells. It is unknown how iron, after its import into the cytosol, is specifically delivered to iron-dependent processes in various cellular compartments. Here, we identify an essential function of the conserved cytosolic monothiol glutaredoxins Grx3 and Grx4 in intracellular iron trafficking and sensing. Depletion of Grx3/4 specifically impaired all iron-requiring reactions in the cytosol, mitochondria, and nucleus, including the synthesis of Fe/S clusters, heme, and di-iron centers. These defects were caused by impairment of iron insertion into proteins and iron transfer to mitochondria, indicating that intracellular iron is not bioavailable, despite highly elevated cytosolic levels. The crucial task of Grx3/4 is mediated by a bridging, glutathione-containing Fe/S center that functions both as an iron sensor and in intracellular iron delivery. Collectively, our study uncovers an important role of monothiol glutaredoxins in cellular iron metabolism, with a surprising connection to cellular redox and sulfur metabolisms.
DOI: 10.1016/j.cmet.2010.08.001
PubMed: 20889129
PubMed Central: PMC4714545
Affiliations:
- Allemagne, Espagne, France, États-Unis
- Auvergne-Rhône-Alpes, Catalogne, District de Giessen, Hesse (Land), Massachusetts, Rhône-Alpes
- Grenoble, Marbourg
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Godoy</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Uzarska, Marta A" sort="Uzarska, Marta A" uniqKey="Uzarska M" first="Marta A" last="Uzarska">Marta A. Uzarska</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Richter, Nadine" sort="Richter, Nadine" uniqKey="Richter N" first="Nadine" last="Richter">Nadine Richter</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Seubert, Andreas" sort="Seubert, Andreas" uniqKey="Seubert A" first="Andreas" last="Seubert">Andreas Seubert</name><affiliation wicri:level="3"><nlm:affiliation>Fachbereich Chemie, Philipps-Universität Marburg, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Fachbereich Chemie, Philipps-Universität Marburg, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Zhang, Yan" sort="Zhang, Yan" uniqKey="Zhang Y" first="Yan" last="Zhang">Yan Zhang</name><affiliation wicri:level="2"><nlm:affiliation>Chemistry Department, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Chemistry Department, Massachusetts Institute of Technology, Cambridge, MA 02139</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Stubbe, Joanne" sort="Stubbe, Joanne" uniqKey="Stubbe J" first="Joanne" last="Stubbe">Joanne Stubbe</name><affiliation wicri:level="2"><nlm:affiliation>Chemistry Department, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Chemistry Department, Massachusetts Institute of Technology, Cambridge, MA 02139</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Pierrel, Fabien" sort="Pierrel, Fabien" uniqKey="Pierrel F" first="Fabien" last="Pierrel">Fabien Pierrel</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Chimie et Biologie des Métaux, CEA Grenoble, 38054 Grenoble Cedex 9, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Chimie et Biologie des Métaux, CEA Grenoble, 38054 Grenoble Cedex 9</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Grenoble</settlement></placeName></affiliation></author><author><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name><affiliation wicri:level="2"><nlm:affiliation>Departament de Ciències Mèdiques Bàsiques, IRB Lleida, Universitat de Lleida, Lleida 25198, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departament de Ciències Mèdiques Bàsiques, IRB Lleida, Universitat de Lleida, Lleida 25198</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany. Electronic address: lill@staff.uni-marburg.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author></analytic><series><title level="j">Cell metabolism</title><idno type="eISSN">1932-7420</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological Transport (MeSH)</term><term>Cytosol (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Iron (metabolism)</term><term>Iron-Sulfur Proteins (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Proteins (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sulfur (metabolism)</term><term>Yeasts (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cytosol (métabolisme)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (MeSH)</term><term>Glutarédoxines (métabolisme)</term><term>Levures (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Soufre (métabolisme)</term><term>Transport biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Iron</term><term>Oxidoreductases</term><term>Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Yeasts</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term><term>Fer</term><term>Glutarédoxines</term><term>Levures</term><term>Oxidoreductases</term><term>Protéines</term><term>Protéines de Saccharomyces cerevisiae</term><term>Soufre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Transport</term><term>Iron-Sulfur Proteins</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Oxydoréduction</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron is an essential nutrient for cells. It is unknown how iron, after its import into the cytosol, is specifically delivered to iron-dependent processes in various cellular compartments. Here, we identify an essential function of the conserved cytosolic monothiol glutaredoxins Grx3 and Grx4 in intracellular iron trafficking and sensing. Depletion of Grx3/4 specifically impaired all iron-requiring reactions in the cytosol, mitochondria, and nucleus, including the synthesis of Fe/S clusters, heme, and di-iron centers. These defects were caused by impairment of iron insertion into proteins and iron transfer to mitochondria, indicating that intracellular iron is not bioavailable, despite highly elevated cytosolic levels. The crucial task of Grx3/4 is mediated by a bridging, glutathione-containing Fe/S center that functions both as an iron sensor and in intracellular iron delivery. Collectively, our study uncovers an important role of monothiol glutaredoxins in cellular iron metabolism, with a surprising connection to cellular redox and sulfur metabolisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20889129</PMID><DateCompleted><Year>2011</Year><Month>02</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1932-7420</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>4</Issue><PubDate><Year>2010</Year><Month>Oct</Month><Day>06</Day></PubDate></JournalIssue><Title>Cell metabolism</Title><ISOAbbreviation>Cell Metab</ISOAbbreviation></Journal><ArticleTitle>Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster.</ArticleTitle><Pagination><MedlinePgn>373-385</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1550-4131(10)00266-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cmet.2010.08.001</ELocationID><Abstract><AbstractText>Iron is an essential nutrient for cells. It is unknown how iron, after its import into the cytosol, is specifically delivered to iron-dependent processes in various cellular compartments. Here, we identify an essential function of the conserved cytosolic monothiol glutaredoxins Grx3 and Grx4 in intracellular iron trafficking and sensing. Depletion of Grx3/4 specifically impaired all iron-requiring reactions in the cytosol, mitochondria, and nucleus, including the synthesis of Fe/S clusters, heme, and di-iron centers. These defects were caused by impairment of iron insertion into proteins and iron transfer to mitochondria, indicating that intracellular iron is not bioavailable, despite highly elevated cytosolic levels. The crucial task of Grx3/4 is mediated by a bridging, glutathione-containing Fe/S center that functions both as an iron sensor and in intracellular iron delivery. Collectively, our study uncovers an important role of monothiol glutaredoxins in cellular iron metabolism, with a surprising connection to cellular redox and sulfur metabolisms.</AbstractText><CopyrightInformation>Copyright © 2010 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mühlenhoff</LastName><ForeName>Ulrich</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Molik</LastName><ForeName>Sabine</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Godoy</LastName><ForeName>José R</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Uzarska</LastName><ForeName>Marta A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Richter</LastName><ForeName>Nadine</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Seubert</LastName><ForeName>Andreas</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Fachbereich Chemie, Philipps-Universität Marburg, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Chemistry Department, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stubbe</LastName><ForeName>JoAnne</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Chemistry Department, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pierrel</LastName><ForeName>Fabien</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratoire de Chimie et Biologie des Métaux, CEA Grenoble, 38054 Grenoble Cedex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, IRB Lleida, Universitat de Lleida, Lleida 25198, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, 35032 Marburg, Germany. Electronic address: lill@staff.uni-marburg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM081393</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM29295</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Metab</MedlineTA><NlmUniqueID>101233170</NlmUniqueID><ISSNLinking>1550-4131</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516012">Grx4 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="C545181">Grx3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Cell Metab. 2014 Oct 7;20(4):696</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015003" MajorTopicYN="N">Yeasts</DescriptorName><QualifierName UI="Q000378" 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Uzarska</name></country><country name="États-Unis"><region name="Massachusetts"><name sortKey="Zhang, Yan" sort="Zhang, Yan" uniqKey="Zhang Y" first="Yan" last="Zhang">Yan Zhang</name></region><name sortKey="Stubbe, Joanne" sort="Stubbe, Joanne" uniqKey="Stubbe J" first="Joanne" last="Stubbe">Joanne Stubbe</name></country><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Pierrel, Fabien" sort="Pierrel, Fabien" uniqKey="Pierrel F" first="Fabien" last="Pierrel">Fabien Pierrel</name></region></country><country name="Espagne"><region name="Catalogne"><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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