Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation.
Identifieur interne : 000775 ( Main/Exploration ); précédent : 000774; suivant : 000776Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation.
Auteurs : Petra Haunhorst [Allemagne] ; Eva-Maria Hanschmann ; Lars Br Utigam ; Oliver Stehling ; Bastian Hoffmann ; Ulrich Mühlenhoff ; Roland Lill ; Carsten Berndt ; Christopher Horst LilligSource :
- Molecular biology of the cell [ 1939-4586 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules HeLa (MeSH), Danio zébré (embryologie), Danio zébré (génétique), Danio zébré (métabolisme), Données de séquences moléculaires (MeSH), Embryon non mammalien (embryologie), Embryon non mammalien (métabolisme), Fer (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Homéostasie (MeSH), Humains (MeSH), Hémoglobines (métabolisme), Interférence par ARN (MeSH), Microscopie de fluorescence (MeSH), Protéine-1 de régulation du fer (métabolisme), Protéine-2 de régulation du fer (métabolisme), Protéines de poisson-zèbre (génétique), Protéines de poisson-zèbre (métabolisme), Protéines de transport (génétique), Protéines de transport (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- embryologie : Danio zébré, Embryon non mammalien.
- génétique : Danio zébré, Glutarédoxines, Protéines de poisson-zèbre, Protéines de transport.
- métabolisme : Danio zébré, Embryon non mammalien, Fer, Glutarédoxines, Hémoglobines, Protéine-1 de régulation du fer, Protéine-2 de régulation du fer, Protéines de poisson-zèbre, Protéines de transport.
- Animaux, Cellules HeLa, Données de séquences moléculaires, Homéostasie, Humains, Interférence par ARN, Microscopie de fluorescence, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Carrier Proteins (genetics), Carrier Proteins (metabolism), Embryo, Nonmammalian (embryology), Embryo, Nonmammalian (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), HeLa Cells (MeSH), Hemoglobins (metabolism), Homeostasis (MeSH), Humans (MeSH), Iron (metabolism), Iron Regulatory Protein 1 (metabolism), Iron Regulatory Protein 2 (metabolism), Microscopy, Fluorescence (MeSH), Molecular Sequence Data (MeSH), RNA Interference (MeSH), Sequence Homology, Amino Acid (MeSH), Zebrafish (embryology), Zebrafish (genetics), Zebrafish (metabolism), Zebrafish Proteins (genetics), Zebrafish Proteins (metabolism).
- MESH :
- chemical , genetics : Carrier Proteins, Glutaredoxins, Zebrafish Proteins.
- chemical , metabolism : Carrier Proteins, Glutaredoxins, Hemoglobins, Iron, Iron Regulatory Protein 1, Iron Regulatory Protein 2, Zebrafish Proteins.
- embryology : Embryo, Nonmammalian, Zebrafish.
- genetics : Zebrafish.
- metabolism : Embryo, Nonmammalian, Zebrafish.
- Amino Acid Sequence, Animals, Base Sequence, HeLa Cells, Homeostasis, Humans, Microscopy, Fluorescence, Molecular Sequence Data, RNA Interference, Sequence Homology, Amino Acid.
Abstract
The mechanisms by which eukaryotic cells handle and distribute the essential micronutrient iron within the cytosol and other cellular compartments are only beginning to emerge. The yeast monothiol multidomain glutaredoxins (Grx) 3 and 4 are essential for both transcriptional iron regulation and intracellular iron distribution. Despite the fact that the mechanisms of iron metabolism differ drastically in fungi and higher eukaryotes, the glutaredoxins are conserved, yet their precise function in vertebrates has remained elusive. Here we demonstrate a crucial role of the vertebrate-specific monothiol multidomain Grx3 (PICOT) in cellular iron homeostasis. During zebrafish embryonic development, depletion of Grx3 severely impairs the maturation of hemoglobin, the major iron-consuming process. Silencing of human Grx3 expression in HeLa cells decreases the activities of several cytosolic Fe/S proteins, for example, iron-regulatory protein 1, a major component of posttranscriptional iron regulation. As a consequence, Grx3-depleted cells show decreased levels of ferritin and increased levels of transferrin receptor, features characteristic of cellular iron starvation. Apparently, Grx3-deficient cells are unable to efficiently use iron, despite unimpaired cellular iron uptake. These data suggest an evolutionarily conserved role of cytosolic monothiol multidomain glutaredoxins in cellular iron metabolism pathways, including the biogenesis of Fe/S proteins and hemoglobin maturation.
DOI: 10.1091/mbc.E12-09-0648
PubMed: 23615448
PubMed Central: PMC3681695
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(genetics)</term><term>Zebrafish (metabolism)</term><term>Zebrafish Proteins (genetics)</term><term>Zebrafish Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules HeLa (MeSH)</term><term>Danio zébré (embryologie)</term><term>Danio zébré (génétique)</term><term>Danio zébré (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Embryon non mammalien (embryologie)</term><term>Embryon non mammalien (métabolisme)</term><term>Fer (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Humains (MeSH)</term><term>Hémoglobines (métabolisme)</term><term>Interférence par ARN (MeSH)</term><term>Microscopie de fluorescence (MeSH)</term><term>Protéine-1 de régulation du fer (métabolisme)</term><term>Protéine-2 de régulation du fer (métabolisme)</term><term>Protéines de poisson-zèbre (génétique)</term><term>Protéines de 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Nonmammalian</term><term>Zebrafish</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Zebrafish</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Danio zébré</term><term>Glutarédoxines</term><term>Protéines de poisson-zèbre</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Embryo, Nonmammalian</term><term>Zebrafish</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Danio zébré</term><term>Embryon non mammalien</term><term>Fer</term><term>Glutarédoxines</term><term>Hémoglobines</term><term>Protéine-1 de régulation du fer</term><term>Protéine-2 de régulation du fer</term><term>Protéines de poisson-zèbre</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>HeLa Cells</term><term>Homeostasis</term><term>Humans</term><term>Microscopy, Fluorescence</term><term>Molecular Sequence Data</term><term>RNA Interference</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Données de séquences moléculaires</term><term>Homéostasie</term><term>Humains</term><term>Interférence par ARN</term><term>Microscopie de fluorescence</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mechanisms by which eukaryotic cells handle and distribute the essential micronutrient iron within the cytosol and other cellular compartments are only beginning to emerge. The yeast monothiol multidomain glutaredoxins (Grx) 3 and 4 are essential for both transcriptional iron regulation and intracellular iron distribution. Despite the fact that the mechanisms of iron metabolism differ drastically in fungi and higher eukaryotes, the glutaredoxins are conserved, yet their precise function in vertebrates has remained elusive. Here we demonstrate a crucial role of the vertebrate-specific monothiol multidomain Grx3 (PICOT) in cellular iron homeostasis. During zebrafish embryonic development, depletion of Grx3 severely impairs the maturation of hemoglobin, the major iron-consuming process. Silencing of human Grx3 expression in HeLa cells decreases the activities of several cytosolic Fe/S proteins, for example, iron-regulatory protein 1, a major component of posttranscriptional iron regulation. As a consequence, Grx3-depleted cells show decreased levels of ferritin and increased levels of transferrin receptor, features characteristic of cellular iron starvation. Apparently, Grx3-deficient cells are unable to efficiently use iron, despite unimpaired cellular iron uptake. These data suggest an evolutionarily conserved role of cytosolic monothiol multidomain glutaredoxins in cellular iron metabolism pathways, including the biogenesis of Fe/S proteins and hemoglobin maturation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23615448</PMID><DateCompleted><Year>2014</Year><Month>01</Month><Day>17</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>12</Issue><PubDate><Year>2013</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation.</ArticleTitle><Pagination><MedlinePgn>1895-903</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E12-09-0648</ELocationID><Abstract><AbstractText>The mechanisms by which eukaryotic cells handle and distribute the essential micronutrient iron within the cytosol and other cellular compartments are only beginning to emerge. The yeast monothiol multidomain glutaredoxins (Grx) 3 and 4 are essential for both transcriptional iron regulation and intracellular iron distribution. Despite the fact that the mechanisms of iron metabolism differ drastically in fungi and higher eukaryotes, the glutaredoxins are conserved, yet their precise function in vertebrates has remained elusive. Here we demonstrate a crucial role of the vertebrate-specific monothiol multidomain Grx3 (PICOT) in cellular iron homeostasis. During zebrafish embryonic development, depletion of Grx3 severely impairs the maturation of hemoglobin, the major iron-consuming process. Silencing of human Grx3 expression in HeLa cells decreases the activities of several cytosolic Fe/S proteins, for example, iron-regulatory protein 1, a major component of posttranscriptional iron regulation. As a consequence, Grx3-depleted cells show decreased levels of ferritin and increased levels of transferrin receptor, features characteristic of cellular iron starvation. Apparently, Grx3-deficient cells are unable to efficiently use iron, despite unimpaired cellular iron uptake. These data suggest an evolutionarily conserved role of cytosolic monothiol multidomain glutaredoxins in cellular iron metabolism pathways, including the biogenesis of Fe/S proteins and hemoglobin maturation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Haunhorst</LastName><ForeName>Petra</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institute for Clinical Cytobiology and Cytopathology, Faculty of Medicine, Philipps-Universität, 35037 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hanschmann</LastName><ForeName>Eva-Maria</ForeName><Initials>EM</Initials></Author><Author ValidYN="Y"><LastName>Bräutigam</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Stehling</LastName><ForeName>Oliver</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Hoffmann</LastName><ForeName>Bastian</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Mühlenhoff</LastName><ForeName>Ulrich</ForeName><Initials>U</Initials></Author><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>04</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Biol Cell</MedlineTA><NlmUniqueID>9201390</NlmUniqueID><ISSNLinking>1059-1524</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C404105">GLRX3 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006454">Hemoglobins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029961">Zebrafish Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D035941">Iron Regulatory Protein 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D035942">Iron Regulatory Protein 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004625" MajorTopicYN="N">Embryo, Nonmammalian</DescriptorName><QualifierName UI="Q000196" MajorTopicYN="N">embryology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006454" MajorTopicYN="N">Hemoglobins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="Y">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></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="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D035942" MajorTopicYN="N">Iron Regulatory Protein 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015027" MajorTopicYN="N">Zebrafish</DescriptorName><QualifierName UI="Q000196" MajorTopicYN="N">embryology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029961" MajorTopicYN="N">Zebrafish Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>1</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23615448</ArticleId><ArticleId IdType="pii">mbc.E12-09-0648</ArticleId><ArticleId IdType="doi">10.1091/mbc.E12-09-0648</ArticleId><ArticleId 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C" first="Carsten" last="Berndt">Carsten Berndt</name><name sortKey="Br Utigam, Lars" sort="Br Utigam, Lars" uniqKey="Br Utigam L" first="Lars" last="Br Utigam">Lars Br Utigam</name><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name><name sortKey="Hoffmann, Bastian" sort="Hoffmann, Bastian" uniqKey="Hoffmann B" first="Bastian" last="Hoffmann">Bastian Hoffmann</name><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><name sortKey="Muhlenhoff, Ulrich" sort="Muhlenhoff, Ulrich" uniqKey="Muhlenhoff U" first="Ulrich" last="Mühlenhoff">Ulrich Mühlenhoff</name><name sortKey="Stehling, Oliver" sort="Stehling, Oliver" uniqKey="Stehling O" first="Oliver" 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