Evidence map›Paper›PMID 28655775›Full record

ArticleThe Journal of biological chemistry2017

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.

Izumi Yanatori, Des R Richardson, Shinya Toyokuni, Fumio Kishi

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Genomic Insights into Vector-Pathogen Adaptation inPathogens (Basel, Switzerland) · 2025
    Article
  8. Cellular Iron Homeostasis.Advances in experimental medicine and biology · 2025
    Review
  9. Review
  10. Mechanisms controlling cellular and systemic iron homeostasis.Nature reviews. Molecular cell biology · 2024
    Review
  11. Article
  12. Environmental impact on carcinogenesis under BRCA1 haploinsufficiency.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2023
    Review
  13. Review
  14. Review
  15. Review
  16. Iron as spirit of life to share under monopoly.Journal of clinical biochemistry and nutrition · 2022
    Article
  17. Article
  18. Review
  19. Review
  20. Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Izumi YanatoriFrom the Department of Molecular Genetics, Kawasaki Medical School, 577 Matsushima, Kurashiki, Okayama 701-0192, Japan.
Des R Richardsonthe Molecular Pharmacology and Pathology Program, Department of Pathology, University of Sydney, Sydney, New South Wales 2006, Australia, and.
Shinya Toyokunithe Molecular Pharmacology and Pathology Program, Department of Pathology, University of Sydney, Sydney, New South Wales 2006, Australia, and.
Fumio KishiFrom the Department of Molecular Genetics, Kawasaki Medical School, 577 Matsushima, Kurashiki, Okayama 701-0192, Japan, fkishi-ygc@umin.ac.jp.
Kawasaki Medical School · JPNagoya University · JPUniversity of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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,

Indexed as

Amino Acid SubstitutionBinding, CompetitiveBinding SitesBiological TransportCell LineGene DeletionHemeHeme Oxygenase-1Heme Oxygenase (Decyclizing)HumansIronMetalloporphyrinsMutationNADPH-Ferrihemoprotein ReductaseProtein Interaction Domains and MotifsProtein MultimerizationDMRT1 proteinHemeHeme Oxygenase-1heme oxygenase-2Heme Oxygenase (Decyclizing)HMOX1 protein, humanIronMetalloporphyrinsNADPH-Ferrihemoprotein ReductasePCBP2 protein, humanRecombinant Fusion ProteinsRNA-Binding Proteinstin mesoporphyrinTranscription Factorshemeheme oxygenaseironiron chaperoneiron metabolismPCBP2protein/protein interaction

Identifiers

PMID28655775
PMCPMC5555184
OpenAlexW2724653687

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.