Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET.
Identifieur interne : 000237 ( Main/Exploration ); précédent : 000236; suivant : 000238Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET.
Auteurs : Nhan Huynh [Canada] ; Qiuxiang Ou [Canada] ; Pendleton Cox [Canada] ; Roland Lill [Allemagne] ; Kirst King-Jones [Canada]Source :
- Nature communications [ 2041-1723 ] ; 2019.
Descripteurs français
- KwdFr :
- 1,4-alpha-Glucan branching enzyme (génétique), 1,4-alpha-Glucan branching enzyme (métabolisme), ARN messager (métabolisme), Animaux (MeSH), Drosophila (MeSH), Ecdystéroïdes (biosynthèse), Fer (métabolisme), Ferrosulfoprotéines (métabolisme), Glandes endocrines (métabolisme), Hème (métabolisme), Larve (métabolisme), Porphyries (génétique), Porphyries (métabolisme), Protéine-1 de régulation du fer (génétique), Protéine-1 de régulation du fer (métabolisme), Protéines de Drosophila (génétique), Protéines de Drosophila (métabolisme), Protéines mitochondriales (génétique), Protéines mitochondriales (métabolisme), Régulation de l'expression des gènes (génétique), Régulation négative (MeSH), Techniques de knock-in de gènes (MeSH), Techniques de knock-out de gènes (MeSH), Transport nucléaire actif (MeSH).
- MESH :
- biosynthèse : Ecdystéroïdes.
- génétique : 1,4-alpha-Glucan branching enzyme, Porphyries, Protéine-1 de régulation du fer, Protéines de Drosophila, Protéines mitochondriales, Régulation de l'expression des gènes.
- métabolisme : 1,4-alpha-Glucan branching enzyme, ARN messager, Fer, Ferrosulfoprotéines, Glandes endocrines, Hème, Larve, Porphyries, Protéine-1 de régulation du fer, Protéines de Drosophila, Protéines mitochondriales.
- Animaux, Drosophila, Régulation négative, Techniques de knock-in de gènes, Techniques de knock-out de gènes, Transport nucléaire actif.
English descriptors
- KwdEn :
- 1,4-alpha-Glucan Branching Enzyme (genetics), 1,4-alpha-Glucan Branching Enzyme (metabolism), Active Transport, Cell Nucleus (MeSH), Animals (MeSH), Down-Regulation (MeSH), Drosophila (MeSH), Drosophila Proteins (genetics), Drosophila Proteins (metabolism), Ecdysteroids (biosynthesis), Endocrine Glands (metabolism), Gene Expression Regulation (genetics), Gene Knock-In Techniques (MeSH), Gene Knockout Techniques (MeSH), Heme (metabolism), Iron (metabolism), Iron Regulatory Protein 1 (genetics), Iron Regulatory Protein 1 (metabolism), Iron-Sulfur Proteins (metabolism), Larva (metabolism), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Porphyrias (genetics), Porphyrias (metabolism), RNA, Messenger (metabolism).
- MESH :
- chemical , biosynthesis : Ecdysteroids.
- chemical , genetics : 1,4-alpha-Glucan Branching Enzyme, Drosophila Proteins, Iron Regulatory Protein 1, Mitochondrial Proteins.
- chemical , metabolism : 1,4-alpha-Glucan Branching Enzyme, Drosophila Proteins, Heme, Iron, Iron Regulatory Protein 1, Iron-Sulfur Proteins, Mitochondrial Proteins, RNA, Messenger.
- genetics : Gene Expression Regulation, Porphyrias.
- metabolism : Endocrine Glands, Larva, Porphyrias.
- Active Transport, Cell Nucleus, Animals, Down-Regulation, Drosophila, Gene Knock-In Techniques, Gene Knockout Techniques.
Abstract
Iron Regulatory Protein 1 (IRP1) is a bifunctional cytosolic iron sensor. When iron levels are normal, IRP1 harbours an iron-sulphur cluster (holo-IRP1), an enzyme with aconitase activity. When iron levels fall, IRP1 loses the cluster (apo-IRP1) and binds to iron-responsive elements (IREs) in messenger RNAs (mRNAs) encoding proteins involved in cellular iron uptake, distribution, and storage. Here we show that mutations in the Drosophila 1,4-Alpha-Glucan Branching Enzyme (AGBE) gene cause porphyria. AGBE was hitherto only linked to glycogen metabolism and a fatal human disorder known as glycogen storage disease type IV. AGBE binds specifically to holo-IRP1 and to mitoNEET, a protein capable of repairing IRP1 iron-sulphur clusters. This interaction ensures nuclear translocation of holo-IRP1 and downregulation of iron-dependent processes, demonstrating that holo-IRP1 functions not just as an aconitase, but throttles target gene expression in anticipation of declining iron requirements.
DOI: 10.1038/s41467-019-13237-8
PubMed: 31784520
PubMed Central: PMC6884552
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9</wicri:regionArea><wicri:noRegion>T6G 2E9</wicri:noRegion></affiliation></author></analytic><series><title level="j">Nature communications</title><idno type="eISSN">2041-1723</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1,4-alpha-Glucan Branching Enzyme (genetics)</term><term>1,4-alpha-Glucan Branching Enzyme (metabolism)</term><term>Active Transport, Cell Nucleus (MeSH)</term><term>Animals (MeSH)</term><term>Down-Regulation (MeSH)</term><term>Drosophila (MeSH)</term><term>Drosophila Proteins (genetics)</term><term>Drosophila Proteins (metabolism)</term><term>Ecdysteroids (biosynthesis)</term><term>Endocrine Glands (metabolism)</term><term>Gene Expression Regulation (genetics)</term><term>Gene Knock-In Techniques (MeSH)</term><term>Gene Knockout Techniques (MeSH)</term><term>Heme (metabolism)</term><term>Iron (metabolism)</term><term>Iron Regulatory Protein 1 (genetics)</term><term>Iron Regulatory Protein 1 (metabolism)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Larva (metabolism)</term><term>Mitochondrial Proteins (genetics)</term><term>Mitochondrial Proteins (metabolism)</term><term>Porphyrias (genetics)</term><term>Porphyrias (metabolism)</term><term>RNA, Messenger (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>1,4-alpha-Glucan branching enzyme (génétique)</term><term>1,4-alpha-Glucan branching enzyme (métabolisme)</term><term>ARN messager (métabolisme)</term><term>Animaux (MeSH)</term><term>Drosophila (MeSH)</term><term>Ecdystéroïdes (biosynthèse)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Glandes endocrines (métabolisme)</term><term>Hème (métabolisme)</term><term>Larve (métabolisme)</term><term>Porphyries (génétique)</term><term>Porphyries (métabolisme)</term><term>Protéine-1 de régulation du fer (génétique)</term><term>Protéine-1 de régulation du fer (métabolisme)</term><term>Protéines de Drosophila (génétique)</term><term>Protéines de Drosophila (métabolisme)</term><term>Protéines mitochondriales (génétique)</term><term>Protéines mitochondriales (métabolisme)</term><term>Régulation de l'expression des gènes (génétique)</term><term>Régulation négative (MeSH)</term><term>Techniques de knock-in de gènes (MeSH)</term><term>Techniques de knock-out de gènes (MeSH)</term><term>Transport nucléaire actif (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Ecdysteroids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>1,4-alpha-Glucan Branching Enzyme</term><term>Drosophila Proteins</term><term>Iron Regulatory Protein 1</term><term>Mitochondrial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>1,4-alpha-Glucan Branching Enzyme</term><term>Drosophila Proteins</term><term>Heme</term><term>Iron</term><term>Iron Regulatory Protein 1</term><term>Iron-Sulfur Proteins</term><term>Mitochondrial Proteins</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Ecdystéroïdes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Gene Expression Regulation</term><term>Porphyrias</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>1,4-alpha-Glucan branching enzyme</term><term>Porphyries</term><term>Protéine-1 de régulation du fer</term><term>Protéines de Drosophila</term><term>Protéines mitochondriales</term><term>Régulation de l'expression des gènes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endocrine Glands</term><term>Larva</term><term>Porphyrias</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>1,4-alpha-Glucan branching enzyme</term><term>ARN messager</term><term>Fer</term><term>Ferrosulfoprotéines</term><term>Glandes endocrines</term><term>Hème</term><term>Larve</term><term>Porphyries</term><term>Protéine-1 de régulation du fer</term><term>Protéines de Drosophila</term><term>Protéines mitochondriales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term><term>Animals</term><term>Down-Regulation</term><term>Drosophila</term><term>Gene Knock-In Techniques</term><term>Gene Knockout Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Drosophila</term><term>Régulation négative</term><term>Techniques de knock-in de gènes</term><term>Techniques de knock-out de gènes</term><term>Transport nucléaire actif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron Regulatory Protein 1 (IRP1) is a bifunctional cytosolic iron sensor. When iron levels are normal, IRP1 harbours an iron-sulphur cluster (holo-IRP1), an enzyme with aconitase activity. When iron levels fall, IRP1 loses the cluster (apo-IRP1) and binds to iron-responsive elements (IREs) in messenger RNAs (mRNAs) encoding proteins involved in cellular iron uptake, distribution, and storage. Here we show that mutations in the Drosophila 1,4-Alpha-Glucan Branching Enzyme (AGBE) gene cause porphyria. AGBE was hitherto only linked to glycogen metabolism and a fatal human disorder known as glycogen storage disease type IV. AGBE binds specifically to holo-IRP1 and to mitoNEET, a protein capable of repairing IRP1 iron-sulphur clusters. This interaction ensures nuclear translocation of holo-IRP1 and downregulation of iron-dependent processes, demonstrating that holo-IRP1 functions not just as an aconitase, but throttles target gene expression in anticipation of declining iron requirements.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31784520</PMID><DateCompleted><Year>2020</Year><Month>03</Month><Day>10</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>10</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>11</Month><Day>29</Day></PubDate></JournalIssue><Title>Nature communications</Title><ISOAbbreviation>Nat Commun</ISOAbbreviation></Journal><ArticleTitle>Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET.</ArticleTitle><Pagination><MedlinePgn>5463</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41467-019-13237-8</ELocationID><Abstract><AbstractText>Iron Regulatory Protein 1 (IRP1) is a bifunctional cytosolic iron sensor. When iron levels are normal, IRP1 harbours an iron-sulphur cluster (holo-IRP1), an enzyme with aconitase activity. When iron levels fall, IRP1 loses the cluster (apo-IRP1) and binds to iron-responsive elements (IREs) in messenger RNAs (mRNAs) encoding proteins involved in cellular iron uptake, distribution, and storage. Here we show that mutations in the Drosophila 1,4-Alpha-Glucan Branching Enzyme (AGBE) gene cause porphyria. AGBE was hitherto only linked to glycogen metabolism and a fatal human disorder known as glycogen storage disease type IV. AGBE binds specifically to holo-IRP1 and to mitoNEET, a protein capable of repairing IRP1 iron-sulphur clusters. This interaction ensures nuclear translocation of holo-IRP1 and downregulation of iron-dependent processes, demonstrating that holo-IRP1 functions not just as an aconitase, but throttles target gene expression in anticipation of declining iron requirements.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huynh</LastName><ForeName>Nhan</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ou</LastName><ForeName>Qiuxiang</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cox</LastName><ForeName>Pendleton</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0002-8345-6518</Identifier><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032, Marburg, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Philipps-Universität Marburg, Hans-Meerwein-Straße, 35043, Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>King-Jones</LastName><ForeName>Kirst</ForeName><Initials>K</Initials><Identifier Source="ORCID">0000-0002-9089-8015</Identifier><AffiliationInfo><Affiliation>Department of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada. kirst.king-jones@ualberta.ca.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MOP 93761</GrantID><Agency>CIHR</Agency><Country>Canada</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nat Commun</MedlineTA><NlmUniqueID>101528555</NlmUniqueID><ISSNLinking>2041-1723</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029721">Drosophila Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026461">Ecdysteroids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.18</RegistryNumber><NameOfSubstance UI="D015061">1,4-alpha-Glucan Branching Enzyme</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="D015061" MajorTopicYN="N">1,4-alpha-Glucan Branching Enzyme</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021581" MajorTopicYN="N">Active Transport, Cell Nucleus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015536" MajorTopicYN="N">Down-Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004330" MajorTopicYN="N">Drosophila</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029721" MajorTopicYN="N">Drosophila Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" 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