How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins.
Identifieur interne : 000112 ( Main/Exploration ); précédent : 000111; suivant : 000113How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins.
Auteurs : Tracey A. Rouault [États-Unis] ; Nunziata Maio [États-Unis]Source :
- Molecular cell [ 1097-4164 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical : F-Box Proteins, Iron, Oxygen, Sulfur, Ubiquitin-Protein Ligase Complexes.
- Homeostasis, Oxidation-Reduction.
Abstract
In this issue of Molecular Cell, Wang et al. (2020) discover that the C-terminal substrate-binding domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes FBXL5 binding to IRP2 to effect its oxygen-dependent degradation, unveiling a novel and previously unrecognized mechanism involved in regulation of cellular iron homeostasis.
DOI: 10.1016/j.molcel.2020.03.020
PubMed: 32243827
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Rouault</name><affiliation wicri:level="2"><nlm:affiliation>Metals Biology and Molecular Medicine Group, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD, USA. 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(2020) discover that the C-terminal substrate-binding domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes FBXL5 binding to IRP2 to effect its oxygen-dependent degradation, unveiling a novel and previously unrecognized mechanism involved in regulation of cellular iron homeostasis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Automated" Owner="NLM"><PMID Version="1">32243827</PMID><DateCompleted><Year>2020</Year><Month>07</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-4164</ISSN><JournalIssue CitedMedium="Internet"><Volume>78</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>04</Month><Day>02</Day></PubDate></JournalIssue><Title>Molecular cell</Title><ISOAbbreviation>Mol Cell</ISOAbbreviation></Journal><ArticleTitle>How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins.</ArticleTitle><Pagination><MedlinePgn>1-3</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1097-2765(20)30188-X</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.molcel.2020.03.020</ELocationID><Abstract><AbstractText>In this issue of Molecular Cell, Wang et al. (2020) discover that the C-terminal substrate-binding domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes FBXL5 binding to IRP2 to effect its oxygen-dependent degradation, unveiling a novel and previously unrecognized mechanism involved in regulation of cellular iron homeostasis.</AbstractText><CopyrightInformation>Published by Elsevier Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouault</LastName><ForeName>Tracey A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>Metals Biology and Molecular Medicine Group, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD, USA. 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Rouault</name></region><name sortKey="Maio, Nunziata" sort="Maio, Nunziata" uniqKey="Maio N" first="Nunziata" last="Maio">Nunziata Maio</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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