Cellular iron sensing and regulation: Nuclear IRP1 extends a classic paradigm.
Identifieur interne : 000162 ( Main/Exploration ); précédent : 000161; suivant : 000163Cellular iron sensing and regulation: Nuclear IRP1 extends a classic paradigm.
Auteurs : Anna Karen Hernández-Gallardo [Mexique] ; Fanis Missirlis [Mexique]Source :
- Biochimica et biophysica acta. Molecular cell research [ 1879-2596 ] ; 2020.
Descripteurs français
- KwdFr :
- ARN messager (génétique), Aconitate hydratase (génétique), Cytosol (métabolisme), Céruloplasmine (génétique), Fer (métabolisme), Ferritines (génétique), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (génétique), Noyau de la cellule (génétique), Oxydoréduction (MeSH), Protéine-1 de régulation du fer (génétique), Protéines régulatrices du fer (génétique), Régulation de l'expression des gènes (génétique).
- MESH :
- composition chimique : Ferrosulfoprotéines.
- génétique : ARN messager, Aconitate hydratase, Céruloplasmine, Ferritines, Ferrosulfoprotéines, Noyau de la cellule, Protéine-1 de régulation du fer, Protéines régulatrices du fer, Régulation de l'expression des gènes.
- métabolisme : Cytosol, Fer.
- Oxydoréduction.
English descriptors
- KwdEn :
- Aconitate Hydratase (genetics), Cell Nucleus (genetics), Ceruloplasmin (genetics), Cytosol (metabolism), Ferritins (genetics), Gene Expression Regulation (genetics), Iron (metabolism), Iron Regulatory Protein 1 (genetics), Iron-Regulatory Proteins (genetics), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Oxidation-Reduction (MeSH), RNA, Messenger (genetics).
- MESH :
- chemical , chemistry : Iron-Sulfur Proteins.
- chemical , genetics : Aconitate Hydratase, Ceruloplasmin, Ferritins, Iron Regulatory Protein 1, Iron-Regulatory Proteins, Iron-Sulfur Proteins, RNA, Messenger.
- genetics : Cell Nucleus, Gene Expression Regulation.
- metabolism : Cytosol, Iron.
- Oxidation-Reduction.
Abstract
The classic view is that iron regulatory proteins operate at the post-transcriptional level. Iron Regulatory Protein 1 (IRP1) shifts between an apo-form that binds mRNAs and a holo-form that harbors a [4Fe4S] cluster. The latter form is not considered relevant to iron regulation, but rather thought to act as a non-essential cytosolic aconitase. Recent work in Drosophila, however, shows that holo-IRP1 can also translocate to the nucleus, where it appears to downregulate iron metabolism genes, preparing the cell for a decline in iron uptake. The shifting of IRP1 between states requires a functional mitoNEET pathway that includes a glycogen branching enzyme for the repair or disassembly of IRP1's oxidatively damaged [3Fe4S] cluster. The new findings add to the notion that glucose metabolism is modulated by iron metabolism. Furthermore, we propose that ferritin ferroxidase activity participates in the repair of the IRP1 [3Fe4S] cluster leading to the hypothesis that cytosolic ferritin directly contributes to cellular iron sensing.
DOI: 10.1016/j.bbamcr.2020.118705
PubMed: 32199885
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Iron Regulatory Protein 1 (IRP1) shifts between an apo-form that binds mRNAs and a holo-form that harbors a [4Fe4S] cluster. The latter form is not considered relevant to iron regulation, but rather thought to act as a non-essential cytosolic aconitase. Recent work in Drosophila, however, shows that holo-IRP1 can also translocate to the nucleus, where it appears to downregulate iron metabolism genes, preparing the cell for a decline in iron uptake. The shifting of IRP1 between states requires a functional mitoNEET pathway that includes a glycogen branching enzyme for the repair or disassembly of IRP1's oxidatively damaged [3Fe4S] cluster. The new findings add to the notion that glucose metabolism is modulated by iron metabolism. Furthermore, we propose that ferritin ferroxidase activity participates in the repair of the IRP1 [3Fe4S] cluster leading to the hypothesis that cytosolic ferritin directly contributes to cellular iron sensing.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32199885</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>23</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-2596</ISSN><JournalIssue CitedMedium="Internet"><Volume>1867</Volume><Issue>7</Issue><PubDate><Year>2020</Year><Month>07</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Molecular cell research</Title><ISOAbbreviation>Biochim Biophys Acta Mol Cell Res</ISOAbbreviation></Journal><ArticleTitle>Cellular iron sensing and regulation: Nuclear IRP1 extends a classic paradigm.</ArticleTitle><Pagination><MedlinePgn>118705</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0167-4889(20)30063-X</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamcr.2020.118705</ELocationID><Abstract><AbstractText>The classic view is that iron regulatory proteins operate at the post-transcriptional level. Iron Regulatory Protein 1 (IRP1) shifts between an apo-form that binds mRNAs and a holo-form that harbors a [4Fe4S] cluster. The latter form is not considered relevant to iron regulation, but rather thought to act as a non-essential cytosolic aconitase. Recent work in Drosophila, however, shows that holo-IRP1 can also translocate to the nucleus, where it appears to downregulate iron metabolism genes, preparing the cell for a decline in iron uptake. The shifting of IRP1 between states requires a functional mitoNEET pathway that includes a glycogen branching enzyme for the repair or disassembly of IRP1's oxidatively damaged [3Fe4S] cluster. The new findings add to the notion that glucose metabolism is modulated by iron metabolism. Furthermore, we propose that ferritin ferroxidase activity participates in the repair of the IRP1 [3Fe4S] cluster leading to the hypothesis that cytosolic ferritin directly contributes to cellular iron sensing.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hernández-Gallardo</LastName><ForeName>Anna Karen</ForeName><Initials>AK</Initials><AffiliationInfo><Affiliation>Departamento de Fisiología, Biofísica y Neurociencias, Cinvestav, CDMX, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Missirlis</LastName><ForeName>Fanis</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Departamento de Fisiología, Biofísica y Neurociencias, Cinvestav, CDMX, Mexico. Electronic address: fanis@fisio.cinvestav.mx.</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><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>03</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Mol Cell Res</MedlineTA><NlmUniqueID>101731731</NlmUniqueID><ISSNLinking>0167-4889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D035925">Iron-Regulatory Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-73-2</RegistryNumber><NameOfSubstance UI="D005293">Ferritins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.16.3.1</RegistryNumber><NameOfSubstance UI="D002570">Ceruloplasmin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D035941">Iron Regulatory Protein 1</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002570" MajorTopicYN="N">Ceruloplasmin</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005293" MajorTopicYN="N">Ferritins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D035941" MajorTopicYN="N">Iron Regulatory Protein 1</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D035925" MajorTopicYN="N">Iron-Regulatory Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Glycogen storage disease</Keyword><Keyword MajorTopicYN="Y">Heme</Keyword><Keyword MajorTopicYN="Y">IRP2</Keyword><Keyword MajorTopicYN="Y">Iron-sulfur cluster</Keyword><Keyword MajorTopicYN="Y">Prothoracic gland</Keyword><Keyword MajorTopicYN="Y">Steroidogenesis</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>01</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>03</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32199885</ArticleId><ArticleId IdType="pii">S0167-4889(20)30063-X</ArticleId><ArticleId IdType="doi">10.1016/j.bbamcr.2020.118705</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Mexique</li></country></list><tree><country name="Mexique"><noRegion><name sortKey="Hernandez Gallardo, Anna Karen" sort="Hernandez Gallardo, Anna Karen" uniqKey="Hernandez Gallardo A" first="Anna Karen" last="Hernández-Gallardo">Anna Karen Hernández-Gallardo</name></noRegion><name sortKey="Missirlis, Fanis" sort="Missirlis, Fanis" uniqKey="Missirlis F" first="Fanis" last="Missirlis">Fanis 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