{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360292619697208832.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1074/jbc.m117.776021"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925820385501?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925820385501?httpAccept=text/plain"}},{"identifier":{"@type":"URI","@value":"https://syndication.highwire.org/content/doi/10.1074/jbc.M117.776021"}},{"identifier":{"@type":"PMID","@value":"28655775"}}],"dc:title":[{"@value":"The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer"}],"description":[{"notation":[{"@value":"Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Moreover, intestinal iron is incorporated as ferrous iron, which is transported via the iron importer, divalent metal transporter 1 (DMT1). Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1. To promote intracellular iron flux, an iron chaperone may be essential for receiving iron generated by heme catabolism, but this hypothesis is untested so far. Herein, we demonstrate that HO1 binds to PCBP2, but not to other PCBP family members, namely PCBP1, PCBP3, or PCBP4. Interestingly, HO1 formed a complex with either CPR or PCBP2, and it was demonstrated that PCBP2 competes with CPR for HO1 binding. Using PCBP2-deletion mutants, we demonstrated that the PCBP2 K homology 3 domain is important for the HO1/PCBP2 interaction. In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Furthermore,"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380292619697208835","@type":"Researcher","foaf:name":[{"@value":"Izumi Yanatori"}]},{"@id":"https://cir.nii.ac.jp/crid/1380292619697208832","@type":"Researcher","foaf:name":[{"@value":"Des R. Richardson"}]},{"@id":"https://cir.nii.ac.jp/crid/1380292619697208834","@type":"Researcher","foaf:name":[{"@value":"Shinya Toyokuni"}]},{"@id":"https://cir.nii.ac.jp/crid/1380292619697208833","@type":"Researcher","foaf:name":[{"@value":"Fumio Kishi"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219258"}],"prism:publicationName":[{"@value":"Journal of Biological Chemistry"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"2017-08","prism:volume":"292","prism:number":"32","prism:startingPage":"13205","prism:endingPage":"13229"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/","http://creativecommons.org/licenses/by/4.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S0021925820385501?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S0021925820385501?httpAccept=text/plain"},{"@id":"https://syndication.highwire.org/content/doi/10.1074/jbc.M117.776021"}],"createdAt":"2017-06-28","modifiedAt":"2022-01-04","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Metalloporphyrins","dc:title":"Metalloporphyrins"},{"@id":"https://cir.nii.ac.jp/all?q=Iron","dc:title":"Iron"},{"@id":"https://cir.nii.ac.jp/all?q=Recombinant%20Fusion%20Proteins","dc:title":"Recombinant Fusion Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Heme","dc:title":"Heme"},{"@id":"https://cir.nii.ac.jp/all?q=Binding,%20Competitive","dc:title":"Binding, Competitive"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Line","dc:title":"Cell Line"},{"@id":"https://cir.nii.ac.jp/all?q=Humans","dc:title":"Humans"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Interaction%20Domains%20and%20Motifs","dc:title":"Protein Interaction Domains and Motifs"},{"@id":"https://cir.nii.ac.jp/all?q=NADPH-Ferrihemoprotein%20Reductase","dc:title":"NADPH-Ferrihemoprotein Reductase"},{"@id":"https://cir.nii.ac.jp/all?q=Binding%20Sites","dc:title":"Binding Sites"},{"@id":"https://cir.nii.ac.jp/all?q=RNA-Binding%20Proteins","dc:title":"RNA-Binding Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Biological%20Transport","dc:title":"Biological Transport"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Transport","dc:title":"Protein Transport"},{"@id":"https://cir.nii.ac.jp/all?q=Amino%20Acid%20Substitution","dc:title":"Amino Acid Substitution"},{"@id":"https://cir.nii.ac.jp/all?q=Structural%20Homology,%20Protein","dc:title":"Structural Homology, Protein"},{"@id":"https://cir.nii.ac.jp/all?q=Heme%20Oxygenase%20(Decyclizing)","dc:title":"Heme Oxygenase (Decyclizing)"},{"@id":"https://cir.nii.ac.jp/all?q=Mutation","dc:title":"Mutation"},{"@id":"https://cir.nii.ac.jp/all?q=RNA%20Interference","dc:title":"RNA Interference"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Multimerization","dc:title":"Protein Multimerization"},{"@id":"https://cir.nii.ac.jp/all?q=Gene%20Deletion","dc:title":"Gene Deletion"},{"@id":"https://cir.nii.ac.jp/all?q=Heme%20Oxygenase-1","dc:title":"Heme Oxygenase-1"},{"@id":"https://cir.nii.ac.jp/all?q=Transcription%20Factors","dc:title":"Transcription Factors"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050863705679667072","@type":"Article","resourceType":"学術雑誌論文(journal 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