Cited by 69Heme Oxygenase-1 and Carbon MonoxideHemoglobin structure and functionIron Metabolism and Disorders

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

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Yanatori, Izumi, Richardson, Des R., Toyokuni, Shinya, Kishi, Fumio·2017·Journal of Biological Chemistry

Abstract

reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1. These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.

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Crossref · 10.1074/jbc.m117.776021

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  • PCBP2 accepts ferrous iron, acts as a chaperone and accompanies iron to the basolateral membrane.

    “Therein, PCBP2 (for poly(rC)-binding protein-2) accepts ferrous iron, acts as chaperone and as such accompanies iron to the basolateral membrane (Philpott and Jadhav, 2019;Shi et al., 2008;Yanatori et al., 2017).”

    From Iron in infection and immunity (2020) · cites this paper as Yanatori et al., 2017

    The paper states that PCBP2 receives ferrous iron, functions as an iron chaperone, and can transfer iron to ferroportin (Abstract and Discussion; page numbers unavailable). It does not specify that PCBP2 accompanies iron to the basolateral membrane, so that location is not supported by our copy. (LLM, conf=0.86)

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Authors
Yanatori, I., Richardson, D. R., Toyokuni, S., & Kishi, F.
Affiliations
  • Kawasaki Medical School (JP)
  • The University of Sydney (AU)
Corresponding author
Kishi, Fumio
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2017-08
Volume
292
Issue
32
Pages
13205-13229
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2724653687
Cited by
69
References
100
Citations by year
2026: 5 · 2025: 7 · 2024: 5 · 2023: 9 · 2022: 7 · 2021: 8 · 2020: 8 · 2019: 10 · 2018: 9 · 2017: 1
FWCI
3.13
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Griffith Research Online (submittedVersion, cc-by)
Funders
  • Japan Agency for Medical Research and Development (Research Program on Hepatitis)
  • National Health and Medical Research Council (APP1128152, APP1060482, APP1062607)
  • Japan Society for the Promotion of Science (Invitation Fellowship & 22591052)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords
heme oxygenase-1, NADPH-cytochrome P450 reductase, heme degradation, iron transfer, metabolon, ferrous iron, iron chaperone, protein-protein interaction
MeSH terms
Binding Sites, Binding, Competitive, Biological Transport, Cell Line, Heme, Heme Oxygenase (Decyclizing), Humans, Iron, Metalloporphyrins, Mutation, NADPH-Ferrihemoprotein Reductase, Recombinant Fusion Proteins, Transcription Factors, RNA-Binding Proteins, Gene Deletion, Amino Acid Substitution, Protein Transport, RNA Interference, Structural Homology, Protein, Heme Oxygenase-1, Protein Interaction Domains and Motifs, Protein Multimerization

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