Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism-Review.
Identifieur interne : 000021 ( Main/Exploration ); précédent : 000020; suivant : 000022Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism-Review.
Auteurs : Trnka Daniel [Allemagne] ; Hossain Md Faruq [Allemagne] ; Jordt Laura Magdalena [Allemagne] ; Gellert Manuela [Allemagne] ; Lillig Christopher Horst [Allemagne]Source :
- Molecules (Basel, Switzerland) [ 1420-3049 ] ; 2020.
Abstract
Glutathione (GSH) was initially identified and characterized for its redox properties and later for its contributions to detoxification reactions. Over the past decade, however, the essential contributions of glutathione to cellular iron metabolism have come more and more into focus. GSH is indispensable in mitochondrial iron-sulfur (FeS) cluster biosynthesis, primarily by co-ligating FeS clusters as a cofactor of the CGFS-type (class II) glutaredoxins (Grxs). GSH is required for the export of the yet to be defined FeS precursor from the mitochondria to the cytosol. In the cytosol, it is an essential cofactor, again of the multi-domain CGFS-type Grxs, master players in cellular iron and FeS trafficking. In this review, we summarize the recent advances and progress in this field. The most urgent open questions are discussed, such as the role of GSH in the export of FeS precursors from mitochondria, the physiological roles of the CGFS-type Grx interactions with BolA-like proteins and the cluster transfer between Grxs and recipient proteins.
DOI: 10.3390/molecules25173860
PubMed: 32854270
PubMed Central: PMC7503856
Affiliations:
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Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Laura Magdalena, Jordt" sort="Laura Magdalena, Jordt" uniqKey="Laura Magdalena J" first="Jordt" last="Laura Magdalena">Jordt Laura Magdalena</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald</wicri:regionArea><wicri:noRegion>17475 Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Manuela, Gellert" sort="Manuela, Gellert" uniqKey="Manuela G" first="Gellert" last="Manuela">Gellert Manuela</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald</wicri:regionArea><wicri:noRegion>17475 Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Christopher Horst, Lillig" sort="Christopher Horst, Lillig" uniqKey="Christopher Horst L" first="Lillig" last="Christopher Horst">Lillig Christopher Horst</name><affiliation wicri:level="1"><nlm:affiliation>Christopher Horst Lillig, Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Ferdinand-Sauerbruch-Straße, 17475 Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Christopher Horst Lillig, Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Ferdinand-Sauerbruch-Straße, 17475 Greifswald</wicri:regionArea><wicri:noRegion>17475 Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion><wicri:noRegion>17475 Greifswald</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecules (Basel, Switzerland)</title><idno type="eISSN">1420-3049</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione (GSH) was initially identified and characterized for its redox properties and later for its contributions to detoxification reactions. Over the past decade, however, the essential contributions of glutathione to cellular iron metabolism have come more and more into focus. GSH is indispensable in mitochondrial iron-sulfur (FeS) cluster biosynthesis, primarily by co-ligating FeS clusters as a cofactor of the CGFS-type (class II) glutaredoxins (Grxs). GSH is required for the export of the yet to be defined FeS precursor from the mitochondria to the cytosol. In the cytosol, it is an essential cofactor, again of the multi-domain CGFS-type Grxs, master players in cellular iron and FeS trafficking. In this review, we summarize the recent advances and progress in this field. The most urgent open questions are discussed, such as the role of GSH in the export of FeS precursors from mitochondria, the physiological roles of the CGFS-type Grx interactions with BolA-like proteins and the cluster transfer between Grxs and recipient proteins.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32854270</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1420-3049</ISSN><JournalIssue CitedMedium="Internet"><Volume>25</Volume><Issue>17</Issue><PubDate><Year>2020</Year><Month>Aug</Month><Day>25</Day></PubDate></JournalIssue><Title>Molecules (Basel, Switzerland)</Title><ISOAbbreviation>Molecules</ISOAbbreviation></Journal><ArticleTitle>Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism-Review.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E3860</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/molecules25173860</ELocationID><Abstract><AbstractText>Glutathione (GSH) was initially identified and characterized for its redox properties and later for its contributions to detoxification reactions. Over the past decade, however, the essential contributions of glutathione to cellular iron metabolism have come more and more into focus. GSH is indispensable in mitochondrial iron-sulfur (FeS) cluster biosynthesis, primarily by co-ligating FeS clusters as a cofactor of the CGFS-type (class II) glutaredoxins (Grxs). GSH is required for the export of the yet to be defined FeS precursor from the mitochondria to the cytosol. In the cytosol, it is an essential cofactor, again of the multi-domain CGFS-type Grxs, master players in cellular iron and FeS trafficking. In this review, we summarize the recent advances and progress in this field. The most urgent open questions are discussed, such as the role of GSH in the export of FeS precursors from mitochondria, the physiological roles of the CGFS-type Grx interactions with BolA-like proteins and the cluster transfer between Grxs and recipient proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Daniel</LastName><ForeName>Trnka</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0002-6609-6880</Identifier><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Faruq</LastName><ForeName>Hossain Md</ForeName><Initials>HM</Initials><Identifier Source="ORCID">0000-0002-8346-063X</Identifier><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Laura Magdalena</LastName><ForeName>Jordt</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0002-8228-2229</Identifier><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Manuela</LastName><ForeName>Gellert</ForeName><Initials>G</Initials><Identifier Source="ORCID">0000-0002-2545-7125</Identifier><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Christopher Horst</LastName><ForeName>Lillig</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Christopher Horst Lillig, Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Ferdinand-Sauerbruch-Straße, 17475 Greifswald, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>Li984/3-1, Li984/3-2, Li984/4-1, GRK1947-A1</GrantID><Agency>Deutsche Forschungsgemeinschaft</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>08</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Molecules</MedlineTA><NlmUniqueID>100964009</NlmUniqueID><ISSNLinking>1420-3049</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">iron</Keyword><Keyword 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